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1AC5

CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004185molecular_functionserine-type carboxypeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_id176
Number of Residues1
DetailsMEMBER OF CATALYTIC TRIAD.
ChainResidue
ASER176

site_id383
Number of Residues1
DetailsMEMBER OF CATALYTIC TRIAD.
ChainResidue
AASP383

site_id448
Number of Residues1
DetailsMEMBER OF CATALYTIC TRIAD.
ChainResidue
AHIS448

Functional Information from PROSITE/UniProt
site_idPS00131
Number of Residues8
DetailsCARBOXYPEPT_SER_SER Serine carboxypeptidases, serine active site. LsGESYAG
ChainResidueDetails
ALEU172-GLY179

site_idPS00560
Number of Residues18
DetailsCARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. LtfVsVyNASHmVPfdkS
ChainResidueDetails
ALEU438-SER455

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1469044","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bcr
ChainResidueDetails
AASP383
AGLY76
ATYR177
ASER176
AHIS448

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bcr
ChainResidueDetails
AASP383
AHIS448
ASER176

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PDB entries from 2025-11-05

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