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	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00520

Chain	Residue	Details
A	MET24
A	THR42

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:6248536

Chain	Residue	Details
A	THR2

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: S-glutathionyl cysteine => ECO:0000269|PubMed:6248536

Chain	Residue	Details
A	PHE22

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P35745

Chain	Residue	Details
A	ASN93

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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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