4OJ1

Crystal structure of truncated Acylphosphatase from S. sulfataricus

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 201

Chain	Residue
A	TYR17

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 202

Chain	Residue
A	GLY28
A	PHE29
A	ARG30

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site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 203

Chain	Residue
A	TYR91

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 204

Chain	Residue
A	ARG19
A	TYR21
A	ALA78
A	ASP85

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site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 201

Chain	Residue
B	ASP97
B	PHE98

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL20-ARG30

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

Chain	Residue	Details
A	GLY44-GLY60

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	172
Details	Domain: {"description":"Acylphosphatase-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00520","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"16287076","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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