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7EQX

Crystal structure of an Aedes aegypti procarboxypeptidase B1

Functional Information from GO Data
ChainGOidnamespacecontents
C0004181molecular_functionmetallocarboxypeptidase activity
C0006508biological_processproteolysis
C0008270molecular_functionzinc ion binding
D0004181molecular_functionmetallocarboxypeptidase activity
D0006508biological_processproteolysis
D0008270molecular_functionzinc ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues112
DetailsPropeptide: {"description":"Activation peptide","featureId":"PRO_0000458088","evidences":[{"source":"PubMed","id":"34750241","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues580
DetailsDomain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00730","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34658092","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34750241","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7EQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7EQZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

251801

PDB entries from 2026-04-08

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