1WPX

Crystal structure of carboxypeptidase Y inhibitor complexed with the cognate proteinase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004185	molecular_function	serine-type carboxypeptidase activity
A	0006508	biological_process	proteolysis
B	0000328	cellular_component	fungal-type vacuole lumen
B	0000329	cellular_component	fungal-type vacuole membrane
B	0004867	molecular_function	serine-type endopeptidase inhibitor activity
B	0005515	molecular_function	protein binding
B	0005543	molecular_function	phospholipid binding
B	0005737	cellular_component	cytoplasm
B	0010466	biological_process	negative regulation of peptidase activity
B	0030162	biological_process	regulation of proteolysis
B	0030414	molecular_function	peptidase inhibitor activity
B	0046578	biological_process	regulation of Ras protein signal transduction

Functional Information from PROSITE/UniProt

site_id	PS00131
Number of Residues	8
Details	CARBOXYPEPT_SER_SER Serine carboxypeptidases, serine active site. IaGESYAG

Chain	Residue	Details
A	ILE142-GLY149

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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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site_id	PS01220
Number of Residues	23
Details	PBP Phosphatidylethanolamine-binding protein family signature. FtLVmTDPDaPSktdhkwsefcH

Chain	Residue	Details
B	PHE589-HIS611

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:12473200

Chain	Residue	Details
B	MET501

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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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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1bcr

Chain	Residue	Details
A	GLY53
A	TYR147
A	SER146

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1bcr

Chain	Residue	Details
A	ASP338
A	HIS397

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site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1bcr

Chain	Residue	Details
A	ASP338
A	HIS397
A	SER146

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