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6F02

Crystal structure of human glycosylated kallistatin at 3.0 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0030414molecular_functionpeptidase inhibitor activity
A0031089cellular_componentplatelet dense granule lumen
A0070062cellular_componentextracellular exosome
C0004867molecular_functionserine-type endopeptidase inhibitor activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0030414molecular_functionpeptidase inhibitor activity
C0031089cellular_componentplatelet dense granule lumen
C0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. LRFNRPFLVvI
ChainResidueDetails
ALEU397-ILE407

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Reactive bond"}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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