1hti

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME

Released:

Function and Biology Details

Reactions catalysed:
Glycerone phosphate = methylglyoxal + phosphate
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-157974 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 26.57 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P60174 (Residues: 2-249; Coverage: 100%)
Gene names: TPI, TPI1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 65.81Å b: 75.39Å c: 92.81Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.167 not available
Expression system: Not provided