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1WPX

Crystal structure of carboxypeptidase Y inhibitor complexed with the cognate proteinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004185molecular_functionserine-type carboxypeptidase activity
A0006508biological_processproteolysis
B0000328cellular_componentfungal-type vacuole lumen
B0000329cellular_componentfungal-type vacuole membrane
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005543molecular_functionphospholipid binding
B0005737cellular_componentcytoplasm
B0030162biological_processregulation of proteolysis
B0030414molecular_functionpeptidase inhibitor activity
B0046578biological_processregulation of Ras protein signal transduction
Functional Information from PROSITE/UniProt
site_idPS00131
Number of Residues8
DetailsCARBOXYPEPT_SER_SER Serine carboxypeptidases, serine active site. IaGESYAG
ChainResidueDetails
AILE142-GLY149

site_idPS00560
Number of Residues18
DetailsCARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. FtyLrVfNGGHmVPfdvP
ChainResidueDetails
APHE387-PRO404

site_idPS01220
Number of Residues23
DetailsPBP Phosphatidylethanolamine-binding protein family signature. FtLVmTDPDaPSktdhkwsefcH
ChainResidueDetails
BPHE589-HIS611

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:12473200
ChainResidueDetails
BMET501

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:7727362
ChainResidueDetails
AASP338

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2639680, ECO:0000305|PubMed:7727362
ChainResidueDetails
AHIS397

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|DOI:10.1007/BF02907496
ChainResidueDetails
ACYS341
AMET398

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:28189789
ChainResidueDetails
AASN13

site_idSWS_FT_FI6
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:15713484, ECO:0000269|PubMed:28189789, ECO:0000269|PubMed:7727362
ChainResidueDetails
AASN87
AASN168
AASN368

219869

PDB entries from 2024-05-15

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