PDBe 4poc

X-ray diffraction
1.6Å resolution

Structure of Triosephosphate Isomerase Wild Type human enzyme.

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 254 amino acids
Theoretical weight: 27.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P60174 (Residues: 38-286; Coverage: 87%)
Gene names: TPI, TPI1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 47.92Å b: 48.851Å c: 93.966Å
α: 90° β: 103.66° γ: 90°
R-values:
R R work R free
0.225 0.153 0.187
Expression system: Escherichia coli BL21(DE3)