PDBe 2vom

X-ray diffraction
1.85Å resolution

Structural basis of human triosephosphate isomerase deficiency. Mutation E104D and correlation to solvent perturbation.

Released:

Function and Biology Details

Reaction catalysed:
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 250 amino acids
Theoretical weight: 26.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P60174 (Residues: 39-286; Coverage: 87%)
Gene names: TPI, TPI1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 320.521Å b: 47.288Å c: 68.957Å
α: 90° β: 97.2° γ: 90°
R-values:
R R work R free
0.219 0.219 0.252
Expression system: Escherichia coli BL21