› 4f95

X-ray diffraction
2.07Å resolution

Crystal structure of human inosine triphosphate pyrophosphatase P32T variant

Released:
DOI: 10.2210/pdb4f95/pdb
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PDB entry 4f95 coloured by chain, front view.
PDB entry 4f95 coloured by chain, side view.
PDB entry 4f95 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The human ITPA polymorphic variant P32T is destabilized by the unpacking of the hydrophobic core.
Simone PD, Struble LR, Kellezi A, Brown CA, Grabow CE, Khutsishvili I, Marky LA, Pavlov YI, Borgstahl GE
J Struct Biol 182 197-208 (2013)
PMID: 23528839

Function and Biology Details

Reaction catalysed: 
A nucleoside triphosphate + H(2)O = a nucleotide + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189814 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inosine triphosphate pyrophosphatase Chain: A
Molecule details ›
Chain: A
Length: 197 amino acids
Theoretical weight: 21.75 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

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P21212
Unit cell:
a: 31.02Å b: 104.42Å c: 50.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.234 0.308
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

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

1 mention without citation

The human ITPA polymorphic variant P32T is destabilized by the unpacking of the hydrophobic core.
Simone et al. (2013)

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