› 4hhp

X-ray diffraction
1.5Å resolution

Crystal structure of triosephosphate isomerase from trypanosoma cruzi, mutant e105d

Released:
DOI: 10.2210/pdb4hhp/pdb
PDB entry 4hhp coloured by chain, front view.
PDB entry 4hhp coloured by chain, side view.
PDB entry 4hhp coloured by chain, top view.
Source organism: Trypanosoma cruzi
Primary publication:
Different contribution of conserved amino acids to the global properties of triosephosphate isomerases.
Aguirre Y, Cabrera N, Aguirre B, Pérez-Montfort R, Hernandez-Santoyo A, Reyes-Vivas H, Enríquez-Flores S, de Gómez-Puyou MT, Gómez-Puyou A, Sanchez-Ruiz JM, Costas M
Proteins 82 323-35 (2014)
PMID: 23966267

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156485 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, B
Molecule details ›
Chains: A, B
Length: 251 amino acids
Theoretical weight: 27.35 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P52270 (Residues: 1-251; Coverage: 100%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P1
Unit cell:
a: 38.716Å b: 44.461Å c: 69.043Å
α: 95.02° β: 96.08° γ: 114.69°
R-values:
R R work R free
0.166 0.166 0.196
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

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)
1 more