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1JMO

Crystal Structure of the Heparin Cofactor II-S195A Thrombin Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005788cellular_componentendoplasmic reticulum lumen
A0006935biological_processchemotaxis
A0007596biological_processblood coagulation
A0008201molecular_functionheparin binding
A0070062cellular_componentextracellular exosome
H0004252molecular_functionserine-type endopeptidase activity
H0005509molecular_functioncalcium ion binding
H0006508biological_processproteolysis
H0007596biological_processblood coagulation
L0004252molecular_functionserine-type endopeptidase activity
L0005576cellular_componentextracellular region
L0006508biological_processproteolysis
L0007596biological_processblood coagulation
Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues85
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. gskgpldqlekggetaqsadpqweqlnnknlsmpllpadfhkentvtndwipegeedddyldlekifsedddyidiv......................................DSLSVSPT
ChainResidueDetails
AGLY1-THR85

site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. FTVDRPFLFlI
ChainResidueDetails
APHE450-ILE460

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
HLEU53-CYS58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond => ECO:0000250
ChainResidueDetails
ALEU444
HASP102
HALA195

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER18

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Sulfotyrosine => ECO:0000269|PubMed:12169660
ChainResidueDetails
ATYS60
ATYS73

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN30

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12169660, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN169

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12169660
ChainResidueDetails
AASN368

219140

PDB entries from 2024-05-01

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