6up8

X-ray diffraction
2Å resolution

Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure

Released:
Source organism: Homo sapiens
Primary publication:
Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure.
Arch Biochem Biophys 689 108473 (2020)
PMID: 32585311

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: 252 amino acids
Theoretical weight: 26.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P60174 (Residues: 2-249; Coverage: 100%)
Gene names: TPI, TPI1
Sequence domains: Triosephosphate isomerase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P212121
Unit cell:
a: 64.96Å b: 74.83Å c: 92.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.195 0.253
Expression system: Escherichia coli