› 2vom

X-ray diffraction
1.85Å resolution

Structural basis of human triosephosphate isomerase deficiency. Mutation E104D and correlation to solvent perturbation.

Released:
DOI: 10.2210/pdb2vom/pdb
PDB entry 2vom coloured by chain, front view.
PDB entry 2vom coloured by chain, side view.
PDB entry 2vom coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface.
Rodríguez-Almazán C, Arreola R, Rodríguez-Larrea D, Aguirre-López B, de Gómez-Puyou MT, Pérez-Montfort R, Costas M, Gómez-Puyou A, Torres-Larios A
J Biol Chem 283 23254-63 (2008)
PMID: 18562316

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 250 amino acids
Theoretical weight: 26.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P60174 (Residues: 2-249; Coverage: 100%)
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 22-ID
Spacegroup: C2
Unit cell:
a: 320.521Å b: 47.288Å c: 68.957Å
α: 90° β: 97.2° γ: 90°
R-values:
R R work R free
0.219 0.219 0.252
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

The return of metabolism: biochemistry and physiology of the pentose phosphate pathway.
Stincone et al. (2015)
3 more

6 mentions without citation

Understanding the mechanism of cytochrome P450 3A4: recent advances and remaining problems.
Sevrioukova et al. (2013)
5 more