3BR8

Crystal structure of acylphosphatase from Bacillus subtilis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003998	molecular_function	acylphosphatase activity
A	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 92

Chain	Residue
A	GLN13
A	GLY14
A	GLY16
A	PHE17
A	ARG18
A	ASN36
A	HOH95
A	HOH103
A	HOH173

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 93

Chain	Residue
A	GLY16
A	ARG18
A	TYR19
A	LYS29
A	GLU58
A	LYS61
A	HOH189

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Functional Information from PROSITE/UniProt

site_id	PS00150
Number of Residues	11
Details	ACYLPHOSPHATASE_1 Acylphosphatase signature 1. VdGrVQGVgFR

Chain	Residue	Details
A	VAL8-ARG18

---

site_id	PS00151
Number of Residues	17
Details	ACYLPHOSPHATASE_2 Acylphosphatase signature 2. GWVKNrddGrVeilaeG

Chain	Residue	Details
A	GLY32-GLY48

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	87
Details	Domain: {"description":"Acylphosphatase-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00520","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00520","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20447399","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 2acy

Chain	Residue	Details
A	ARG18
A	ASN36

---