2oma:A    (THR45) to   (GLN225)  CRYSTALLOGRAPHIC ANALYSIS OF A CHEMICALLY MODIFIED TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI WITH DITHIOBENZYLAMINE (DTBA)  |   TRIOSEPHOSPHATE ISOMERASE, TRYPANOSOMA CRUZI, PROTEIN INTERFACES, DITHIOBISBENZYLAMINE, ISOMERASE 
1ag1:O    (LEU48) to   (GLN224)  MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE  |   ISOMERASE (INTRAMOLECULAR OXIDOREDUCTASE), ISOMERASE(INTRAMOLECULAR OXIDOREDUCTSE) 
1ag1:T    (LEU48) to   (GLN224)  MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE  |   ISOMERASE (INTRAMOLECULAR OXIDOREDUCTASE), ISOMERASE(INTRAMOLECULAR OXIDOREDUCTSE) 
1amk:A    (ILE48) to   (ALA224)  LEISHMANIA MEXICANA TRIOSE PHOSPHATE ISOMERASE  |   TIM, 2-PG, PGA, GLUCONEOGENESIS, FATTY ACID BIOSYNTHESIS 
4hhp:A    (ILE49) to   (GLN225)  CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI, MUTANT E105D  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
4hhp:B    (ILE49) to   (GLN225)  CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI, MUTANT E105D  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
3tao:B    (LEU50) to   (GLN230)  STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS TRIOSEPHOSPHATE ISOMERASE BOUND TO PHOSPHOGLYCOLOHYDROXAMATE  |   ISOMERASE 
3tim:A    (LEU48) to   (GLN224)  THE CRYSTAL STRUCTURE OF THE "OPEN" AND THE "CLOSED" CONFORMATION OF THE FLEXIBLE LOOP OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTSE) 
3tim:B    (LEU48) to   (GLN225)  THE CRYSTAL STRUCTURE OF THE "OPEN" AND THE "CLOSED" CONFORMATION OF THE FLEXIBLE LOOP OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTSE) 
4y9a:A    (PRO50) to   (LYS234)  CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM STREPTOMYCES COELICOLOR  |   TIM BARREL, ISOMERASE, TPI 
4jeq:A    (LEU48) to   (GLN224)  DIFFERENT CONTRIBUTION OF CONSERVED AMINO ACIDS TO THE GLOBAL PROPERTIES OF HOMOLOGOUS ENZYMES  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
4jeq:B    (LEU48) to   (GLN224)  DIFFERENT CONTRIBUTION OF CONSERVED AMINO ACIDS TO THE GLOBAL PROPERTIES OF HOMOLOGOUS ENZYMES  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
4jeq:C    (LEU48) to   (GLN224)  DIFFERENT CONTRIBUTION OF CONSERVED AMINO ACIDS TO THE GLOBAL PROPERTIES OF HOMOLOGOUS ENZYMES  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
4jeq:D    (LEU48) to   (GLN224)  DIFFERENT CONTRIBUTION OF CONSERVED AMINO ACIDS TO THE GLOBAL PROPERTIES OF HOMOLOGOUS ENZYMES  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
4jeq:F    (LEU48) to   (GLN225)  DIFFERENT CONTRIBUTION OF CONSERVED AMINO ACIDS TO THE GLOBAL PROPERTIES OF HOMOLOGOUS ENZYMES  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
4jeq:G    (LEU48) to   (GLN225)  DIFFERENT CONTRIBUTION OF CONSERVED AMINO ACIDS TO THE GLOBAL PROPERTIES OF HOMOLOGOUS ENZYMES  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
4jeq:H    (LEU48) to   (GLN224)  DIFFERENT CONTRIBUTION OF CONSERVED AMINO ACIDS TO THE GLOBAL PROPERTIES OF HOMOLOGOUS ENZYMES  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
4jeq:I    (LEU48) to   (GLN225)  DIFFERENT CONTRIBUTION OF CONSERVED AMINO ACIDS TO THE GLOBAL PROPERTIES OF HOMOLOGOUS ENZYMES  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
4jeq:J    (LEU48) to   (GLN224)  DIFFERENT CONTRIBUTION OF CONSERVED AMINO ACIDS TO THE GLOBAL PROPERTIES OF HOMOLOGOUS ENZYMES  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
4jeq:K    (THR44) to   (GLN225)  DIFFERENT CONTRIBUTION OF CONSERVED AMINO ACIDS TO THE GLOBAL PROPERTIES OF HOMOLOGOUS ENZYMES  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
4jeq:L    (LEU48) to   (GLN224)  DIFFERENT CONTRIBUTION OF CONSERVED AMINO ACIDS TO THE GLOBAL PROPERTIES OF HOMOLOGOUS ENZYMES  |   TIM BARREL, ISOMERASE, DISEASE MUTATION, PENTOSE SHUNT, GLUCONEOGENESIS, GLYCOLYSIS 
1qds:A    (ILE48) to   (ALA224)  SUPERSTABLE E65Q MUTANT OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE (TIM)  |   TIM, LEISHMANIA, STABILITY, MUTAGENESIS, PKA, ISOMERASE 
4ymz:A    (LEU49) to   (LYS228)  DHAP BOUND LEPTOSPIRA INTERROGANS TRIOSEPHOSPHATE ISOMERASE (LITIM)  |   TIM BARRELS, BETA-ALPHA BARRELS, ISOMERASE, DIHYDROXYACETONE PHOSPHATE, GLYCOLYSIS 
4ymz:B    (LEU49) to   (LYS228)  DHAP BOUND LEPTOSPIRA INTERROGANS TRIOSEPHOSPHATE ISOMERASE (LITIM)  |   TIM BARRELS, BETA-ALPHA BARRELS, ISOMERASE, DIHYDROXYACETONE PHOSPHATE, GLYCOLYSIS 
2v0t:A    (LEU48) to   (GLN224)  THE A178L MUTATION IN THE C-TERMINAL HINGE OF THE FLEXIBLE LOOP-6 OF TRIOSEPHOSPHATE ISOMERASE (TIM) INDUCES A MORE CLOSED CONFORMATION OF THIS HINGE REGION IN DIMERIC AND MONOMERIC TIM  |   ISOMERASE, SOMERASE, TIM-BARREL 
2v0t:B    (LEU48) to   (GLN224)  THE A178L MUTATION IN THE C-TERMINAL HINGE OF THE FLEXIBLE LOOP-6 OF TRIOSEPHOSPHATE ISOMERASE (TIM) INDUCES A MORE CLOSED CONFORMATION OF THIS HINGE REGION IN DIMERIC AND MONOMERIC TIM  |   ISOMERASE, SOMERASE, TIM-BARREL 
2v0t:C    (LEU48) to   (GLN224)  THE A178L MUTATION IN THE C-TERMINAL HINGE OF THE FLEXIBLE LOOP-6 OF TRIOSEPHOSPHATE ISOMERASE (TIM) INDUCES A MORE CLOSED CONFORMATION OF THIS HINGE REGION IN DIMERIC AND MONOMERIC TIM  |   ISOMERASE, SOMERASE, TIM-BARREL 
2v0t:E    (LEU48) to   (GLN225)  THE A178L MUTATION IN THE C-TERMINAL HINGE OF THE FLEXIBLE LOOP-6 OF TRIOSEPHOSPHATE ISOMERASE (TIM) INDUCES A MORE CLOSED CONFORMATION OF THIS HINGE REGION IN DIMERIC AND MONOMERIC TIM  |   ISOMERASE, SOMERASE, TIM-BARREL 
2v0t:F    (LEU48) to   (GLN224)  THE A178L MUTATION IN THE C-TERMINAL HINGE OF THE FLEXIBLE LOOP-6 OF TRIOSEPHOSPHATE ISOMERASE (TIM) INDUCES A MORE CLOSED CONFORMATION OF THIS HINGE REGION IN DIMERIC AND MONOMERIC TIM  |   ISOMERASE, SOMERASE, TIM-BARREL 
2v0t:G    (LEU48) to   (GLN224)  THE A178L MUTATION IN THE C-TERMINAL HINGE OF THE FLEXIBLE LOOP-6 OF TRIOSEPHOSPHATE ISOMERASE (TIM) INDUCES A MORE CLOSED CONFORMATION OF THIS HINGE REGION IN DIMERIC AND MONOMERIC TIM  |   ISOMERASE, SOMERASE, TIM-BARREL 
2v5b:A    (ILE49) to   (GLN225)  THE MONOMERIZATION OF TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI  |   TIM, UNFOLDING, MONOTCTIM, ISOMERASE, GLYCOSOME, GLUCONEOGENESIS, LIPID SYNTHESIS, MONOMERIC MUTANT, GLYCOLYSIS, PENTOSE SHUNT, MONOMERIZATION, FATTY ACID BIOSYNTHESIS, TRIOSEPHOSPHATE ISOMERASE 
2v5l:A    (LEU48) to   (GLN225)  STRUCTURES OF THE OPEN AND CLOSED STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE: AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM  |   OXIDOREDUCTASE, TRIOSEPHOSPHATE ISOMERASE, PENTOSE SHUNT, GLUCONEOGENESIS, BINDING STUDIES, TIM, ISOMERASE, GLYCOSOME, GLYCOLYSIS, ENGINEERING, LIPID SYNTHESIS, FATTY ACID BIOSYNTHESIS 
2v5l:B   (LEU348) to   (GLN524)  STRUCTURES OF THE OPEN AND CLOSED STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE: AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM  |   OXIDOREDUCTASE, TRIOSEPHOSPHATE ISOMERASE, PENTOSE SHUNT, GLUCONEOGENESIS, BINDING STUDIES, TIM, ISOMERASE, GLYCOSOME, GLYCOLYSIS, ENGINEERING, LIPID SYNTHESIS, FATTY ACID BIOSYNTHESIS 
2vei:B    (LEU48) to   (ARG226)  STRUCTURE-BASED ENZYME ENGINEERING EFFORTS WITH AN INACTIVE MONOMERIC TIM VARIANT: THE IMPORTANCE OF A SINGLE POINT MUTATION FOR GENERATING AN ACTIVE SITE WITH SUITABLE BINDING PROPERTIES  |   ISOMERASE, TRIOSEPHOSPHATE ISOMERASE, TIM BARREL, GLYCOLYSIS, ENGINEERING, PENTOSE SHUNT, BINDING POCKET, GLUCONEOGENESIS, LIPID SYNTHESIS, SUBSTRATE SPECIFICITY, FATTY ACID BIOSYNTHESIS, TIM, ENZYME, MONOMERIC, GLYCOSOME 
2vei:C    (HIS47) to   (TYR223)  STRUCTURE-BASED ENZYME ENGINEERING EFFORTS WITH AN INACTIVE MONOMERIC TIM VARIANT: THE IMPORTANCE OF A SINGLE POINT MUTATION FOR GENERATING AN ACTIVE SITE WITH SUITABLE BINDING PROPERTIES  |   ISOMERASE, TRIOSEPHOSPHATE ISOMERASE, TIM BARREL, GLYCOLYSIS, ENGINEERING, PENTOSE SHUNT, BINDING POCKET, GLUCONEOGENESIS, LIPID SYNTHESIS, SUBSTRATE SPECIFICITY, FATTY ACID BIOSYNTHESIS, TIM, ENZYME, MONOMERIC, GLYCOSOME 
1tcd:A    (ILE49) to   (GLN225)  TRYPANOSOMA CRUZI TRIOSEPHOSPHATE ISOMERASE  |   ISOMERASE, INTRAMOLECULAR OXIDOREDUCTASE, GLYCOLYSIS, ISOMERIZATION BETWEEN GLYCERALDEHYDE 3-PHOSPHATE AND DIHYDROXYACETONE, ALPHA-BETA BARREL 
1tpd:A    (LEU48) to   (GLN224)  STRUCTURES OF THE "OPEN" AND "CLOSED" STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) 
1tpd:B    (LEU48) to   (GLN224)  STRUCTURES OF THE "OPEN" AND "CLOSED" STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) 
1tpe:A    (LEU48) to   (GLN224)  COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) 
1tpf:A    (LEU48) to   (GLN224)  COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) 
1tpf:B    (LEU48) to   (GLN224)  COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) 
1tsi:A    (LEU48) to   (GLN224)  STRUCTURE OF THE COMPLEX BETWEEN TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE AND N-HYDROXY-4-PHOSPHONO- BUTANAMIDE: BINDING AT THE ACTIVE SITE DESPITE AN "OPEN" FLEXIBLE LOOP  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTSE) 
1tsi:B    (LEU48) to   (GLN224)  STRUCTURE OF THE COMPLEX BETWEEN TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE AND N-HYDROXY-4-PHOSPHONO- BUTANAMIDE: BINDING AT THE ACTIVE SITE DESPITE AN "OPEN" FLEXIBLE LOOP  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTSE) 
1iig:B   (LEU348) to   (GLN524)  STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHONOPROPIONATE  |   TIM LIGAND COMPLEX, ISOMERASE 
1iih:A    (LEU48) to   (GLN224)  STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHOGLYCERATE  |   TIM LIGAND COMPLEX, ISOMERASE 
1iih:B   (LEU348) to   (GLN524)  STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHOGLYCERATE  |   TIM LIGAND COMPLEX, ISOMERASE 
2j27:A    (LEU48) to   (GLN224)  THE FUNCTIONAL ROLE OF THE CONSERVED ACTIVE SITE PROLINE OF TRIOSEPHOSPHATE ISOMERASE  |   TIM, 2PG, LOOP7, ISOMERASE, GLYCOSOME, TIM-BARREL, GLUCONEOGENESIS, LIPID SYNTHESIS, ATOMIC RESOLUTION, GLYCOLYSIS, PENTOSE SHUNT, POINT MUTATION, FATTY ACID BIOSYNTHESIS, 2-PHOSPHO GLYCOLATE, PROTEIN ENGINEERING 
2j27:B    (LEU48) to   (GLN224)  THE FUNCTIONAL ROLE OF THE CONSERVED ACTIVE SITE PROLINE OF TRIOSEPHOSPHATE ISOMERASE  |   TIM, 2PG, LOOP7, ISOMERASE, GLYCOSOME, TIM-BARREL, GLUCONEOGENESIS, LIPID SYNTHESIS, ATOMIC RESOLUTION, GLYCOLYSIS, PENTOSE SHUNT, POINT MUTATION, FATTY ACID BIOSYNTHESIS, 2-PHOSPHO GLYCOLATE, PROTEIN ENGINEERING 
2y61:A  (ILE1048) to  (ALA1224)  CRYSTAL STRUCTURE OF LEISHMANIAL E65Q-TIM COMPLEXED WITH S-GLYCIDOL PHOSPHATE  |   ISOMERASE, FATTY ACID BIOSYNTHESIS, TRANSITION STATE ANALOGUE, GLYCOLYSIS, PENTOSE SHUNT, GLUCONEOGENESIS, ENZYME-LIGAND COMPLEX 
2y62:A  (ILE1048) to  (ALA1224)  CRYSTAL STRUCTURE OF LEISHMANIAL E65Q-TIM COMPLEXED WITH R-GLYCIDOL PHOSPHATE  |   ISOMERASE, FATTY ACID BIOSYNTHESIS, TRANSITION STATE ANALOGUE, GLYCOLYSIS, PENTOSE SHUNT, GLUCONEOGENESIS, ENZYME-LIGAND COMPLEX 
2y6z:A    (ALA69) to   (GLN239)  CRYSTALLOGRAPHIC STRUCTURE OF GM23 AN EXAMPLE OF CATALYTIC MIGRATION FROM TIM TO THIAMIN PHOSPHATE SYNTHASE.  |   ISOMERASE 
1kv5:A    (LEU48) to   (GLN224)  STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TIM WITH THE SALT-BRIDGE- FORMING RESIDUE ARG191 MUTATED TO SER  |   TIM BARREL, MUTANT, SALT BRIDGE, ISOMERASE 
1kv5:B    (LEU48) to   (GLN224)  STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TIM WITH THE SALT-BRIDGE- FORMING RESIDUE ARG191 MUTATED TO SER  |   TIM BARREL, MUTANT, SALT BRIDGE, ISOMERASE 
5cg7:A    (ILE49) to   (MET225)  LEISHMANIA SIAMENSIS TRIOSEPHOSPHATE ISOMERASE  |   TIM BARREL, C2 STRUCTURE, CACODYLATE BINDING CYS57, HYDROLASE 
5cg7:B    (ILE49) to   (MET225)  LEISHMANIA SIAMENSIS TRIOSEPHOSPHATE ISOMERASE  |   TIM BARREL, C2 STRUCTURE, CACODYLATE BINDING CYS57, HYDROLASE 
4pcf:B    (LEU48) to   (GLN224)  STRUCTURE-BASED PROTEIN ENGINEERING OF A MONOMERIC TRIOSEPHOSPHATE ISOMERASE TOWARDS CHANGING SUBSTRATE SPECIFICITY  |   TRIOSEPHOSPHATE ISOMERASE, TIM BARREL, PROTEIN ENGINEERING, SUBSTRATE SPECIFICITY, ISOMERASE 
4pcf:C    (THR44) to   (ARG226)  STRUCTURE-BASED PROTEIN ENGINEERING OF A MONOMERIC TRIOSEPHOSPHATE ISOMERASE TOWARDS CHANGING SUBSTRATE SPECIFICITY  |   TRIOSEPHOSPHATE ISOMERASE, TIM BARREL, PROTEIN ENGINEERING, SUBSTRATE SPECIFICITY, ISOMERASE 
1n55:A    (ILE48) to   (ALA224)  0.83A RESOLUTION STRUCTURE OF THE E65Q MUTANT OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 2-PHOSPHOGLYCOLATE  |   TIM, ATOMIC RESOLUTION, ENZYME-LIGAND COMPLEX, TRANSITION-STATE ANALOGUE, LOW-BARRIER HYDROGEN BOND, ISOMERASE 
4tim:A    (LEU48) to   (GLN224)  CRYSTALLOGRAPHIC AND MOLECULAR MODELING STUDIES ON TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE: A CRITICAL ASSESSMENT OF THE PREDICTED AND OBSERVED STRUCTURES OF THE COMPLEX WITH 2-PHOSPHOGLYCERATE  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) 
4tim:B    (LEU48) to   (GLN224)  CRYSTALLOGRAPHIC AND MOLECULAR MODELING STUDIES ON TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE: A CRITICAL ASSESSMENT OF THE PREDICTED AND OBSERVED STRUCTURES OF THE COMPLEX WITH 2-PHOSPHOGLYCERATE  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) 
5i3h:A    (LEU48) to   (ARG226)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, PGA, ISOMERASE 
5i3h:B    (LEU48) to   (GLN224)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, PGA, ISOMERASE 
5i3f:A    (LEU48) to   (GLN224)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, ISOMERASE 
5i3f:B    (LEU48) to   (GLN224)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, ISOMERASE 
5i3f:C    (LEU48) to   (GLN224)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, ISOMERASE 
5i3f:D    (LEU48) to   (GLN224)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, ISOMERASE 
5i3i:A    (LEU48) to   (GLN224)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, PGA, ISOMERASE 
5i3i:B    (LEU48) to   (GLN224)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, PGA, ISOMERASE 
5i3i:C    (LEU48) to   (GLN225)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, PGA, ISOMERASE 
5i3j:B    (LEU48) to   (GLN224)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, ISOMERASE 
3q37:A    (ILE49) to   (GLN225)  IDENTIFICATION OF AMINO ACIDS THAT ACCOUNT FOR LONG-RANGE INTERACTIONS IN PROTEINS USING TWO TRIOSEPHOSPHATE ISOMERASES FROM PATHOGENIC TRYPANOSOMES.  |   TIM BARREL, ISOMERASE 
3q37:B    (ILE49) to   (GLN225)  IDENTIFICATION OF AMINO ACIDS THAT ACCOUNT FOR LONG-RANGE INTERACTIONS IN PROTEINS USING TWO TRIOSEPHOSPHATE ISOMERASES FROM PATHOGENIC TRYPANOSOMES.  |   TIM BARREL, ISOMERASE 
3q37:C    (ILE49) to   (GLN225)  IDENTIFICATION OF AMINO ACIDS THAT ACCOUNT FOR LONG-RANGE INTERACTIONS IN PROTEINS USING TWO TRIOSEPHOSPHATE ISOMERASES FROM PATHOGENIC TRYPANOSOMES.  |   TIM BARREL, ISOMERASE 
3q37:D    (ILE49) to   (GLN225)  IDENTIFICATION OF AMINO ACIDS THAT ACCOUNT FOR LONG-RANGE INTERACTIONS IN PROTEINS USING TWO TRIOSEPHOSPHATE ISOMERASES FROM PATHOGENIC TRYPANOSOMES.  |   TIM BARREL, ISOMERASE 
4gnj:A    (ILE49) to   (LYS226)  CRYSTAL STRUCTURE ANALYSIS OF LEISHMANIA SIAMENSIS TRIOSEPHOSPHATE ISOMERASE  |   TIM BARREL, ISOMERASE 
4gnj:B    (ILE49) to   (MET225)  CRYSTAL STRUCTURE ANALYSIS OF LEISHMANIA SIAMENSIS TRIOSEPHOSPHATE ISOMERASE  |   TIM BARREL, ISOMERASE 
6tim:B    (LEU48) to   (GLN224)  THE ADAPTABILITY OF THE ACTIVE SITE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE AS OBSERVED IN THE CRYSTAL STRUCTURES OF THREE DIFFERENT COMPLEXES  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) 
4x22:A    (LEU49) to   (LYS228)  CRYSTAL STRUCTURE OF LEPTOSPIRA INTERROGANS TRIOSEPHOSPHATE ISOMERASE (LITIM)  |   TIM BARRELS, BETA-ALPHA BARRELS, ISOMERASE 
2btm:A    (LEU46) to   (GLN224)  DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES?  |   THERMOPHILIC TRIOSE-PHOSPHATE, GLYCOLYSIS, ISOMERASE 
2btm:B    (LEU46) to   (GLN224)  DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES?  |   THERMOPHILIC TRIOSE-PHOSPHATE, GLYCOLYSIS, ISOMERASE 
1ci1:A    (ILE49) to   (GLN225)  CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI IN HEXANE  |   TRIOSEPHOSPHATE ISOMERASE, TRYPANOSOMA CRUZI, ORGANIC SOLVENT, HEXANE, OLIGOMERIC PROTEIN 
2v2c:A    (LEU48) to   (GLN224)  THE A178L MUTATION IN THE C-TERMINAL HINGE OF THE FLEXIBLE LOOP-6 OF TRIOSEPHOSPHATE ISOMERASE (TIM) INDUCES A MORE CLOSED CONFORMATION OF THIS HINGE REGION IN DIMERIC AND MONOMERIC TIM  |   ISOMERASE, GLYCOSOME, TIM-BARREL, GLYCOLYSIS, ENGINEERING, PENTOSE SHUNT, POINT MUTATION, TIM, 2PG, A178L, LOOP6, HINGE, LOOP-6, ENZYME, FATTY ACID BIOSYNTHESIS, TRIOSEPHOSPHATE ISOMERASE, GLUCONEOGENESIS, LIPID SYNTHESIS, 2-PHOSPHO GLYCOLLATE 
1sux:A    (THR45) to   (GLN225)  CRYSTALLOGRAPHIC ANALYSIS OF THE COMPLEX BETWEEN TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI AND 3-(2- BENZOTHIAZOLYLTHIO)-1-PROPANESULFONIC ACID  |   TRIOSEPHOSPHATE ISOMERASE, TRYPANOSOMA CRUZI, PROTEIN INTERFACES, BENZOTHIAZOLE INHIBITOR 
2vxn:A    (ILE48) to   (ALA224)  E65Q-TIM COMPLEXED WITH PHOSPHOGLYCOLOHYDROXAMATE AT 0.82 A RESOLUTION  |   ISOMERASE, FATTY ACID BIOSYNTHESIS, TRANSITION STATE ANALOGUE, GLYCOLYSIS, PENTOSE SHUNT, GLUCONEOGENESIS, TIM, GLYCOSOME, TRIOSEPHOSPHATE ISOMERASE, ENZYME-LIGAND COMPLEX, LIPID SYNTHESIS, TRANSITION STATE, PROTONATION STATE 
1trd:B    (LEU48) to   (GLN224)  THE INFLUENCE OF CRYSTAL PACKING ON CRYSTALLOGRAPHIC BINDING STUDIES: A NEW CRYSTAL FORM OF TRYPANOSOMAL TIM  |   INTRAMOLECULAR OXIDOREDUCTASE 
1ttj:A    (LEU48) to   (GLN224)  THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTIM: CONFORMATIONAL FLEXIBILITY OF LOOP-1,LOOP-4 AND LOOP-8  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) 
1if2:A    (ILE48) to   (ALA224)  X-RAY STRUCTURE OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH IPP  |   TIM BARREL, TRANSITION STATE ANALOGUE, ISOMERASE 
2j24:B    (LEU48) to   (GLN225)  THE FUNCTIONAL ROLE OF THE CONSERVED ACTIVE SITE PROLINE OF TRIOSEPHOSPHATE ISOMERASE  |   ISOMERASE, PROTEIN ENGINEERING, FATTY ACID BIOSYNTHESIS, GLUCONEOGENESIS, LIPID SYNTHESIS, PENTOSE SHUNT, POINT MUTATION, LOOP7, GLYCOSOME, TIM-BARREL 
2y63:A    (ILE48) to   (ALA224)  CRYSTAL STRUCTURE OF LEISHMANIAL E65Q-TIM COMPLEXED WITH BROMOHYDROXYACETONE PHOSPHATE  |   ISOMERASE, FATTY ACID BIOSYNTHESIS, TRANSITION STATE ANALOGUE, GLYCOLYSIS, PENTOSE SHUNT, GLUCONEOGENESIS, TIM, GOP, GLYCOSOME, LIPID SYNTHESIS, TRANSITION STATE 
5i3g:A    (LEU48) to   (TYR223)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, ISOMERASE 
5i3g:B    (LEU48) to   (GLN224)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, ISOMERASE 
5i3g:D    (LEU48) to   (GLN225)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, ISOMERASE 
5i3k:A    (LEU48) to   (GLN225)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, PGA, ISOMERASE 
5i3k:B    (LEU48) to   (GLN224)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, PGA, ISOMERASE 
5i3k:C    (LEU48) to   (GLN224)  STRUCTURE-FUNCTION STUDIES ON ROLE OF HYDROPHOBIC CLAMPING OF A BASIC GLUTAMATE IN CATALYSIS BY TRIOSEPHOSPHATE ISOMERASE  |   TRIOSEPHOSPHATE ISOMERASE, CATALYSIS, HYDROPHOBIC CLAMPING, PGA, ISOMERASE 
5tim:A    (LEU48) to   (GLN224)  REFINED 1.83 ANGSTROMS STRUCTURE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, CRYSTALLIZED IN THE PRESENCE OF 2.4 M-AMMONIUM SULPHATE. A COMPARISON WITH THE STRUCTURE OF THE TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE-GLYCEROL-3- PHOSPHATE COMPLEX  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) 
5tim:B    (LEU48) to   (GLN224)  REFINED 1.83 ANGSTROMS STRUCTURE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, CRYSTALLIZED IN THE PRESENCE OF 2.4 M-AMMONIUM SULPHATE. A COMPARISON WITH THE STRUCTURE OF THE TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE-GLYCEROL-3- PHOSPHATE COMPLEX  |   ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)