Tableau information
Concept source: d4ij5a_ amino acid (a.a.) range (LEU122)(SER171)
nSSEs in this Concept: 4
String of secondary struct.elems. (SSEs) defining this concept: HEHH
Each SSE's a.a.range: (start resi) (end resi) SSEtype (H=Helix; E=Strand) followed by a numeric SSE ID:
(LEU122) (ARG139) H1
(GLN143) (SER149) E2
(THR151) (GLY163) H3
(ASP165) (SER171) H4
Orientation angles° of SSE-pairs; those in contact shown in bold font
H1
E2 161.3° E2
H3 -61.7° 137.0° H3
H4 88.9° -78.4° 127.6°
Footnote: Inferred from this concept's usages (listed below) was the angular variance of 1σ = ±5.6° about each orientation angle shown above.
Loci of concept usages (shown as a range of a.a. residue ids) in SCOP(v2.05) domains, along with their brief legend taken from SCOP
d4ij5a_ : (LEU122) (SER171) [view usage] : c.60.1.0 |Phosphoglycerate mutase-like |Phosphoglycerate mutase-like |automated matches |automated matches |Hydrogenobacter thermophilus [TaxId: 608538]
d1bq3b_ : (SER150) (LYS202) [view usage] : c.60.1.1 |Phosphoglycerate mutase-like |Phosphoglycerate mutase-like |Cofactor-dependent phosphoglycerate mutase |Phosphoglycerate mutase |Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932]
d2z23a_ : (ASP298) (GLY352) [view usage] : c.94.1.1 |Periplasmic binding protein-like II |Periplasmic binding protein-like II |Phosphate binding protein-like |automated matches |Yersinia pestis [TaxId: 214092]
d4ij6a_ : (LEU122) (SER171) [view usage] : c.60.1.0 |Phosphoglycerate mutase-like |Phosphoglycerate mutase-like |automated matches |automated matches |Hydrogenobacter thermophilus [TaxId: 608538]
d2a6pa_ : (SER118) (ARG168) [view usage] : c.60.1.0 |Phosphoglycerate mutase-like |Phosphoglycerate mutase-like |automated matches |automated matches |Mycobacterium tuberculosis [TaxId: 83332]
d4gpic_ : (LEU156) (LEU208) [view usage] : c.60.1.1 |Phosphoglycerate mutase-like |Phosphoglycerate mutase-like |Cofactor-dependent phosphoglycerate mutase |automated matches |Human (Homo sapiens) [TaxId: 9606]
d1yfkb_ : (LEU156) (GLU207) [view usage] : c.60.1.1 |Phosphoglycerate mutase-like |Phosphoglycerate mutase-like |Cofactor-dependent phosphoglycerate mutase |automated matches |Human (Homo sapiens) [TaxId: 9606]
d4aqha_ : (TYR7) (GLY63) [view usage] : e.1.1.1 |Serpins |Serpins |Serpins |automated matches |Human (Homo sapiens) [TaxId: 9606]
d1bq3a_ : (SER150) (LYS202) [view usage] : c.60.1.1 |Phosphoglycerate mutase-like |Phosphoglycerate mutase-like |Cofactor-dependent phosphoglycerate mutase |Phosphoglycerate mutase |Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932]
d1yjxi_ : (SER155) (GLU207) [view usage] : c.60.1.1 |Phosphoglycerate mutase-like |Phosphoglycerate mutase-like |Cofactor-dependent phosphoglycerate mutase |automated matches |Human (Homo sapiens) [TaxId: 9606]
d1yfka_ : (LEU156) (LEU208) [view usage] : c.60.1.1 |Phosphoglycerate mutase-like |Phosphoglycerate mutase-like |Cofactor-dependent phosphoglycerate mutase |automated matches |Human (Homo sapiens) [TaxId: 9606]
d1pkya3 : (ARG353) (PHE391) [view usage] : c.49.1.1 |Pyruvate kinase C-terminal domain-like |PK C-terminal domain-like |Pyruvate kinase, C-terminal domain |Pyruvate kinase, C-terminal domain |Escherichia coli [TaxId: 562]
d4ij6b_ : (LEU122) (PHE172) [view usage] : c.60.1.0 |Phosphoglycerate mutase-like |Phosphoglycerate mutase-like |automated matches |automated matches |Hydrogenobacter thermophilus [TaxId: 608538]
d1gd8a_ : (SER14) (LEU70) [view usage] : d.188.1.1 |Prokaryotic ribosomal protein L17 |Prokaryotic ribosomal protein L17 |Prokaryotic ribosomal protein L17 |Prokaryotic ribosomal protein L17 |Thermus thermophilus [TaxId: 274]
d1yjxf_ : (SER155) (GLU207) [view usage] : c.60.1.1 |Phosphoglycerate mutase-like |Phosphoglycerate mutase-like |Cofactor-dependent phosphoglycerate mutase |automated matches |Human (Homo sapiens) [TaxId: 9606]
d1jmjb_ : (SER102) (HIS163) [view usage] : e.1.1.1 |Serpins |Serpins |Serpins |Heparin cofactor II (Hc-II, leuserpin 2) |Human (Homo sapiens) [TaxId: 9606]
List of distinct SCOP folds where this concept is used (in one or more of its domains):
c.94, c.60, e.1, c.49, d.188