› 1kv5

X-ray diffraction
1.65Å resolution

Structure of Trypanosoma brucei brucei TIM with the salt-bridge-forming residue Arg191 mutated to Ser

Released:
DOI: 10.2210/pdb1kv5/pdb
PDB entry 1kv5 coloured by chain, front view.
PDB entry 1kv5 coloured by chain, side view.
PDB entry 1kv5 coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis.
Kursula I, Partanen S, Lambeir AM, Wierenga RK
FEBS Lett 518 39-42 (2002)
PMID: 11997014

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138176 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 26.8 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04789 (Residues: 1-250; Coverage: 100%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

4 bound ligands:
Ligand PGA 2 x PGA
Ligand DTT 1 x DTT
Ligand GOL 4 x GOL
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P212121
Unit cell:
a: 44.943Å b: 100.638Å c: 109.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.143 0.175
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.
Olivares-Illana et al. (2017)
19 other articles

4 mentions without citation

PocketMatch: a new algorithm to compare binding sites in protein structures.
Yeturu et al. (2008)
3 more