› 4pod

X-ray diffraction
1.99Å resolution

Structure of Triosephosphate Isomerase I170V mutant human enzyme.

Released:
DOI: 10.2210/pdb4pod/pdb
PDB entry 4pod coloured by chain, front view.
PDB entry 4pod coloured by chain, side view.
PDB entry 4pod coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Triosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency.
Roland BP, Amrich CG, Kammerer CJ, Stuchul KA, Larsen SB, Rode S, Aslam AA, Heroux A, Wetzel R, VanDemark AP, Palladino MJ
Biochim Biophys Acta 1852 61-9 (2015)
PMID: 25463631

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
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: 27.21 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

4 bound ligands:
Ligand K 2 x K
Ligand NA 1 x NA
Ligand PO4 1 x PO4
Ligand BR 1 x BR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 63.659Å b: 70.729Å c: 91.749Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.17 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.
Olivares-Illana et al. (2017)
1 more

2 mentions without citation

Triosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency.
Roland et al. (2015)
1 more