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2FHM

Solution Structure of Bacillus subtilis Acylphosphatase

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. VdGrVQGVgFR
ChainResidueDetails
AVAL8-ARG18

site_idPS00151
Number of Residues17
DetailsACYLPHOSPHATASE_2 Acylphosphatase signature 2. GWVKNrddGrVeilaeG
ChainResidueDetails
AGLY32-GLY48

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues87
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":"PROSITE-ProRule","id":"PRU00520","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20447399","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2acy
ChainResidueDetails
AARG18
AASN36

243083

PDB entries from 2025-10-15

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