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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 Residues1
DetailsSITE: Inhibitory (P1) (chymotrypsin, elastase) => ECO:0000250
ChainResidueDetails
AMET36

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Inhibitory (P1) (trypsin) => ECO:0000250
ChainResidueDetails
AARG92

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: O-linked (Xyl...) (chondroitin sulfate) serine => ECO:0000269|PubMed:1898736, ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717, ECO:0000269|PubMed:6171497, ECO:0000269|PubMed:7682553
ChainResidueDetails
ASER10

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:6171497
ChainResidueDetails
AASN45

222624

PDB entries from 2024-07-17

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