1APS

THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS

Functional Information from GO Data

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

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL13-ARG23

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

Chain	Residue	Details
A	GLY37-GLY53

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	90
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	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00520","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"6248536","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"S-glutathionyl cysteine","evidences":[{"source":"PubMed","id":"6248536","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P35745","evidenceCode":"ECO:0000250"}]}

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	ARG23
A	ASN41

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