PDBe 1wyi

X-ray diffraction
2.2Å resolution

human triosephosphate isomerase of new crystal form

Released:
Source organism: Homo sapiens

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

Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 26.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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: SPRING-8 BEAMLINE BL26B2
Spacegroup: P212121
Unit cell:
a: 46.564Å b: 70.883Å c: 141.412Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.266 0.247 0.296
Expression system: Escherichia coli