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1BCR

COMPLEX OF THE WHEAT SERINE CARBOXYPEPTIDASE, CPDW-II, WITH THE MICROBIAL PEPTIDE ALDEHYDE INHIBITOR, ANTIPAIN, AND ARGININE AT ROOM TEMPERATURE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004185molecular_functionserine-type carboxypeptidase activity
A0006508biological_processproteolysis
B0004185molecular_functionserine-type carboxypeptidase activity
B0006508biological_processproteolysis
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. LtlVsVrGAGHeVPlhrP
ChainResidueDetails
BLEU387-PRO404

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"evidences":[{"source":"PubMed","id":"8636973","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7727364","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8636973","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BCS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1WHS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1WHT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1390755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7727364","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8636973","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1WHT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SC2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7727364","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WHT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 7727364, 7727364
ChainResidueDetails
AGLY53
ATYR147
ASER146
BASP338
BHIS397

site_idMCSA1
Number of Residues2
DetailsM-CSA 5
ChainResidueDetails
BASP338electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
BHIS397electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ATYR147electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-11-05

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