PDBe 1xsa

Solution NMR

Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant)

Released:
Source organism: Homo sapiens

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] Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 17.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P50583 (Residues: 1-147; Coverage: 100%)
Gene names: APAH1, NUDT2
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 85%
Refinement method: CANDID with talos for NOE assignments. xplor-NIH with RAMA pot. Further Refine against CACB shifts
Expression system: Escherichia coli BL21(DE3)