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1HLT

THE STRUCTURE OF A NONADECAPEPTIDE OF THE FIFTH EGF DOMAIN OF THROMBOMODULIN COMPLEXED WITH THROMBIN

Functional Information from GO Data
ChainGOidnamespacecontents
H0004252molecular_functionserine-type endopeptidase activity
H0005509molecular_functioncalcium ion binding
H0006508biological_processproteolysis
H0007596biological_processblood coagulation
J0004252molecular_functionserine-type endopeptidase activity
J0005576cellular_componentextracellular region
J0006508biological_processproteolysis
J0007596biological_processblood coagulation
K0004252molecular_functionserine-type endopeptidase activity
K0005509molecular_functioncalcium ion binding
K0006508biological_processproteolysis
K0007596biological_processblood coagulation
L0004252molecular_functionserine-type endopeptidase activity
L0005576cellular_componentextracellular region
L0006508biological_processproteolysis
L0007596biological_processblood coagulation
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 0G6 H 1
ChainResidue
HHIS57
HSER214
HTRP215
HGLY216
HGLY219
HHOH915
HTYR60
HASN98
HLEU99
HILE174
HASP189
HALA190
HCYS191
HSER195

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 0G6 K 1
ChainResidue
KHIS57
KTYR60
KTRP60
KLEU99
KILE174
KASP189
KALA190
KCYS191
KGLY193
KSER195
KSER214
KTRP215
KGLY216
KGLY219

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
HLEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
HASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsRegion: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Charge relay system"}
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"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"873923","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HGLY193
HHIS57

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
KASP102
KSER195
KGLY193
KHIS57

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HHIS57
HGLY196

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
KASP102
KSER195
KHIS57
KGLY196

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HHIS57

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
KASP102
KSER195
KHIS57

246704

PDB entries from 2025-12-24

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