3U53: Crystal Structure Of Human Ap4a Hydrolase

Citation:
Abstract
ApA hydrolase (asymmetrical diadenosine tetraphosphate hydrolase, EC 3.6.1.17), an enzyme involved in a number of biological processes, is characterized as cleaving the polyphosphate chain at the fourth phosphate from the bound adenosine moiety. This paper presents the crystal structure of wild-type and E58A mutant human ApA hydrolase. Similar to the canonical Nudix fold, human ApA hydrolase shows the common alphabetaalpha-sandwich architecture. Interestingly, two sulfate ions and one diphosphate coordinated with some conserved residues were observed in the active cleft, which affords a better understanding of a possible mode of substrate binding.
PDB ID: 3U53Download
MMDB ID: 103725
PDB Deposition Date: 2011/10/10
Updated in MMDB: 2012/10
Experimental Method:
x-ray diffraction
Resolution: 2.71  Å
Source Organism:
Similar Structures:
Biological Unit for 3U53: monomeric; determined by author and by software (PISA)
Molecular Components in 3U53
Label Count Molecule
Protein (1 molecule)
1
Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical](Gene symbol: NUDT2)
Molecule annotation
Chemicals (4 molecules)
1
3
2
1
* Click molecule labels to explore molecular sequence information.

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