PDBe 2jk2

X-ray diffraction
1.7Å resolution

STRUCTURAL BASIS OF HUMAN TRIOSEPHOSPHATE ISOMERASE DEFICIENCY. CRYSTAL STRUCTURE OF THE WILD TYPE ENZYME.

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
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 26.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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 21-ID-F
Spacegroup: P212121
Unit cell:
a: 65.13Å b: 73.06Å c: 92.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.252
Expression system: Escherichia coli BL21(DE3)