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1JMJ

Crystal Structure of Native Heparin Cofactor II

Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005788cellular_componentendoplasmic reticulum lumen
A0006935biological_processchemotaxis
A0007596biological_processblood coagulation
A0007599biological_processhemostasis
A0008201molecular_functionheparin binding
A0030414molecular_functionpeptidase inhibitor activity
A0070062cellular_componentextracellular exosome
B0004866molecular_functionendopeptidase inhibitor activity
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005788cellular_componentendoplasmic reticulum lumen
B0006935biological_processchemotaxis
B0007596biological_processblood coagulation
B0007599biological_processhemostasis
B0008201molecular_functionheparin binding
B0030414molecular_functionpeptidase inhibitor activity
B0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. FTVDRPFLFlI
ChainResidueDetails
APHE450-ILE460

site_idPS00430
Number of Residues85
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. gskgpldqlekggetaqsadpqweqlnnknlsmpllpadfhkentvtndwipegeedddyldlekifsedddyidiv......................................DSLSVSPT
ChainResidueDetails
AGLY1-THR85

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsRegion: {"description":"Glycosaminoglycan-binding site"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Reactive bond","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12169660","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12169660","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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