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Solution NMR

Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant) in complex with ATP

Released:
DOI: 10.2210/pdb1xsc/pdb
PDB entry 1xsc coloured by chain, ensemble of 25 models, front view.
PDB entry 1xsc coloured by chain, ensemble of 25 models, side view.
PDB entry 1xsc coloured by chain, ensemble of 25 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure and substrate-binding mechanism of human Ap4A hydrolase.
Swarbrick JD, Buyya S, Gunawardana D, Gayler KR, McLennan AG, Gooley PR
J Biol Chem 280 8471-81 (2005)
PMID: 15596429

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156228 (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: 2-147; Coverage: 99%)
Gene names: APAH1, NUDT2
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

1 bound ligand:
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: CNS from a starting structure with ATP 20A from binding site, Refine against NOE/CACB no RAMA potential
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Dinucleoside polyphosphates in the eye: from physiology to therapeutics.
Guzmán-Aranguez et al. (2007)
1 more

2 mentions without citation

Structural basis of UGUA recognition by the Nudix protein CFI(m)25 and implications for a regulatory role in mRNA 3' processing.
Yang et al. (2010)
1 more