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4RLD

Crystal structure of kkf mutant of bla G 2 protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0004190molecular_functionaspartic-type endopeptidase activity
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1228
DetailsDomain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15811379","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18519566","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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