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3BR8

Crystal structure of acylphosphatase from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003998molecular_functionacylphosphatase activity
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 92
ChainResidue
AGLN13
AGLY14
AGLY16
APHE17
AARG18
AASN36
AHOH95
AHOH103
AHOH173

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 93
ChainResidue
AGLY16
AARG18
ATYR19
ALYS29
AGLU58
ALYS61
AHOH189

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 Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00520, ECO:0000269|PubMed:20447399
ChainResidueDetails
AARG18
AASN36

220113

PDB entries from 2024-05-22

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