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1BIK

X-RAY STRUCTURE OF BIKUNIN FROM THE HUMAN INTER-ALPHA-INHIBITOR COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FqyGGCmgngnnFvtekeC
ChainResidueDetails
APHE54-CYS72
APHE110-CYS128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues50
DetailsDomain: {"description":"BPTI/Kunitz inhibitor 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues50
DetailsDomain: {"description":"BPTI/Kunitz inhibitor 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Inhibitory (P1) (chymotrypsin, elastase)","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Inhibitory (P1) (trypsin)","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6171497","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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