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1TB6

2.5A Crystal Structure of the Antithrombin-Thrombin-Heparin Ternary Complex

Functional Information from GO Data
ChainGOidnamespacecontents
H0004252molecular_functionserine-type endopeptidase activity
H0005509molecular_functioncalcium ion binding
H0006508biological_processproteolysis
H0007596biological_processblood coagulation
I0002020molecular_functionprotease binding
I0004867molecular_functionserine-type endopeptidase inhibitor activity
I0005515molecular_functionprotein binding
I0005576cellular_componentextracellular region
I0005615cellular_componentextracellular space
I0005788cellular_componentendoplasmic reticulum lumen
I0005886cellular_componentplasma membrane
I0007596biological_processblood coagulation
I0007599biological_processhemostasis
I0008201molecular_functionheparin binding
I0030193biological_processregulation of blood coagulation
I0030414molecular_functionpeptidase inhibitor activity
I0042802molecular_functionidentical protein binding
I0062023cellular_componentcollagen-containing extracellular matrix
I0070062cellular_componentextracellular exosome
I0072562cellular_componentblood microparticle
L0004252molecular_functionserine-type endopeptidase activity
L0005576cellular_componentextracellular region
L0006508biological_processproteolysis
L0007596biological_processblood coagulation
Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. FKANRPFLVfI
ChainResidueDetails
IPHE402-ILE412

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 Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
HHIS57
HASP102
HALA195

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923
ChainResidueDetails
HASN60

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ITHR31

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569
ChainResidueDetails
ISER36

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|Ref.10
ChainResidueDetails
IASN96

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|Ref.10
ChainResidueDetails
IASN135

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|Ref.10
ChainResidueDetails
IASN155

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|Ref.10
ChainResidueDetails
IASN192

218853

PDB entries from 2024-04-24

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