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1XMN

Crystal structure of thrombin bound to heparin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0007596biological_processblood coagulation
B0004252molecular_functionserine-type endopeptidase activity
B0005509molecular_functioncalcium ion binding
B0006508biological_processproteolysis
B0007596biological_processblood coagulation
C0004252molecular_functionserine-type endopeptidase activity
C0005576cellular_componentextracellular region
C0006508biological_processproteolysis
C0007596biological_processblood coagulation
D0004252molecular_functionserine-type endopeptidase activity
D0005509molecular_functioncalcium ion binding
D0006508biological_processproteolysis
D0007596biological_processblood coagulation
E0004252molecular_functionserine-type endopeptidase activity
E0005576cellular_componentextracellular region
E0006508biological_processproteolysis
E0007596biological_processblood coagulation
F0004252molecular_functionserine-type endopeptidase activity
F0005509molecular_functioncalcium ion binding
F0006508biological_processproteolysis
F0007596biological_processblood coagulation
G0004252molecular_functionserine-type endopeptidase activity
G0005576cellular_componentextracellular region
G0006508biological_processproteolysis
G0007596biological_processblood coagulation
H0004252molecular_functionserine-type endopeptidase activity
H0005509molecular_functioncalcium ion binding
H0006508biological_processproteolysis
H0007596biological_processblood coagulation
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
BLEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
BASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BHIS57
HHIS57
HASP102
HSER195
BASP102
BSER195
DHIS57
DASP102
DSER195
FHIS57
FASP102
FSER195

site_idSWS_FT_FI2
Number of Residues4
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
BASN60
DASN60
FASN60
HASN60

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BGLY193
BHIS57

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DHIS57

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
FASP102
FSER195
FHIS57

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HHIS57

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DGLY193
DHIS57

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
FASP102
FSER195
FGLY193
FHIS57

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HGLY193
HHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57
BGLY196

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DHIS57
DGLY196

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
FASP102
FSER195
FHIS57
FGLY196

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HHIS57
HGLY196

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57

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PDB entries from 2024-07-17

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