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4OIX

Crystal structure of truncated Acylphosphatase from S. sulfataricus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003998molecular_functionacylphosphatase activity
A0016787molecular_functionhydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00150
Number of Residues11
DetailsACYLPHOSPHATASE_1 Acylphosphatase signature 1. VyGlVQGVgFR
ChainResidueDetails
AVAL20-ARG30

site_idPS00151
Number of Residues17
DetailsACYLPHOSPHATASE_2 Acylphosphatase signature 2. GYAKNlpdGsVevvaeG
ChainResidueDetails
AGLY44-GLY60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues86
DetailsDomain: {"description":"Acylphosphatase-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00520","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"16287076","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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