› 2j4e

X-ray diffraction
2.8Å resolution

THE ITP COMPLEX OF HUMAN INOSINE TRIPHOSPHATASE

Released:
DOI: 10.2210/pdb2j4e/pdb
PDB entry 2j4e coloured by chain, front view.
PDB entry 2j4e coloured by chain, side view.
PDB entry 2j4e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T.
Stenmark P, Kursula P, Flodin S, Gräslund S, Landry R, Nordlund P, Schüler H
J Biol Chem 282 3182-7 (2007)
PMID: 17138556

Function and Biology Details

Reaction catalysed: 
A nucleoside triphosphate + H(2)O = a nucleotide + diphosphate
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-573604 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inosine triphosphate pyrophosphatase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 196 amino acids
Theoretical weight: 21.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BY32 (Residues: 1-194; Coverage: 100%)
Gene names: C20orf37, ITPA, My049, OK/SW-cl.9
Sequence domains: Ham1 family
Structure domains: Maf protein

Ligands and Environments

4 bound ligands:
Ligand ITT 7 x ITT
Ligand MG 8 x MG
Ligand POP 1 x POP
Ligand IMP 1 x IMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P1
Unit cell:
a: 67.998Å b: 75.292Å c: 110.793Å
α: 85.12° β: 77.72° γ: 69.19°
R-values:
R R work R free
0.204 0.201 0.265
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Pharmacogenetic significance of inosine triphosphatase.
Bierau et al. (2007)
9 more

6 mentions without citation

ITPA (inosine triphosphate pyrophosphatase): from surveillance of nucleotide pools to human disease and pharmacogenetics.
Simone et al. (2013)
5 more