› 2jk2

X-ray diffraction
1.7Å resolution

STRUCTURAL BASIS OF HUMAN TRIOSEPHOSPHATE ISOMERASE DEFICIENCY. CRYSTAL STRUCTURE OF THE WILD TYPE ENZYME.

Released:
DOI: 10.2210/pdb2jk2/pdb
PDB entry 2jk2 coloured by chain, front view.
PDB entry 2jk2 coloured by chain, side view.
PDB entry 2jk2 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 domain:

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: 250 amino acids
Theoretical weight: 26.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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 21-ID-F
Spacegroup: P212121
Unit cell:
a: 65.13Å b: 73.06Å c: 92.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.252
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

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

12 mentions without citation

Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational Modifications.
Enríquez-Flores et al. (2023)
11 more