1CPY

SITE-DIRECTED MUTAGENESIS ON (SERINE) CARBOXYPEPTIDASE Y FROM YEAST. THE SIGNIFICANCE OF THR 60 AND MET 398 IN HYDROLYSIS AND AMINOLYSIS REACTIONS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004185	molecular_function	serine-type carboxypeptidase activity
A	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	CAT
Number of Residues	4
Details

Chain	Residue
A	SER146
A	ASP338
A	HIS397
A	ALA145

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site_id	CBS
Number of Residues	4
Details

Chain	Residue
A	ASN51
A	GLY52
A	ALA145
A	HIS397

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site_id	S1P
Number of Residues	7
Details

Chain	Residue
A	PHE64
A	ALA65
A	TYR256
A	TYR269
A	LEU272
A	MET398
A	THR60

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site_id	S1S
Number of Residues	6
Details

Chain	Residue
A	TYR147
A	LEU178
A	LEU245
A	TRP312
A	ILE340
A	CYS341

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Functional Information from PROSITE/UniProt

site_id	PS00560
Number of Residues	18
Details	CARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. FtyLrVfNGGHmVPfdvP

Chain	Residue	Details
A	PHE387-PRO404

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:7727362, ECO:0000269|DOI:10.1007/BF02907496

Chain	Residue	Details
A	SER146

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:7727362

Chain	Residue	Details
A	ASP338

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site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:2639680, ECO:0000305|PubMed:7727362

Chain	Residue	Details
A	HIS397

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|DOI:10.1007/BF02907496

Chain	Residue	Details
A	CYS341
A	MET398

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:28189789

Chain	Residue	Details
A	ASN13

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site_id	SWS_FT_FI6
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:15713484, ECO:0000269|PubMed:28189789, ECO:0000269|PubMed:7727362

Chain	Residue	Details
A	ASN87
A	ASN168
A	ASN368

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