PDBe 3u53

X-ray diffraction
2.7Å resolution

Crystal structure of human Ap4A hydrolase

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of wild-type and mutant human Ap4A hydrolase.
Biochem. Biophys. Res. Commun. 432 16-21 (2013)
PMID: 23384440

Function and Biology Details

Reaction catalysed:
P(1),P(4)-bis(5'-guanosyl) tetraphosphate + H(2)O = GTP + GMP
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 155 amino acids
Theoretical weight: 17.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P50583 (Residues: 1-147; Coverage: 100%)
Gene names: APAH1, NUDT2
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P43
Unit cell:
a: 72.485Å b: 72.485Å c: 133.491Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.213 0.284
Expression system: Escherichia coli