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X-ray diffraction
1.7Å resolution

Structure of human triose phosphate isomerase K13M

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: 254 amino acids
Theoretical weight: 27.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P60174 (Residues: 1-249; Coverage: 100%)
Gene names: TPI, TPI1
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 65.066Å b: 73.53Å c: 92.816Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.147 0.187
Expression system: Escherichia coli BL21(DE3)