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1A0H

THE X-RAY CRYSTAL STRUCTURE OF PPACK-MEIZOTHROMBIN DESF1: KRINGLE/THROMBIN AND CARBOHYDRATE/KRINGLE/THROMBIN INTERACTIONS AND LOCATION OF THE LINKER CHAIN

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
D0004252molecular_functionserine-type endopeptidase activity
D0005576cellular_componentextracellular region
D0006508biological_processproteolysis
D0007596biological_processblood coagulation
E0004252molecular_functionserine-type endopeptidase activity
E0005509molecular_functioncalcium ion binding
E0006508biological_processproteolysis
E0007596biological_processblood coagulation
Functional Information from PROSITE/UniProt
site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. FCRNpdgdeegaWC
ChainResidueDetails
APHE218-CYS231

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
BLEU359-CYS364

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
BASP519-VAL530

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues156
DetailsDomain: {"description":"Kringle 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Cleavage; by factor Xa","evidences":[{"source":"UniProtKB","id":"P00734","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues508
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues44
DetailsRegion: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1975","firstPage":"25","lastPage":"46","publisher":"Leiden University Press","address":"Leiden","bookName":"Boerhaave symposium on prothrombin and related coagulation factors","editors":["Hemker H.C.","Veltkamp J.J."],"authors":["Magnusson S.","Sottrup-Jensen L.","Petersen T.E.","Claeys H."]}}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP419
BSER525
BGLY523
BHIS363

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASP419
ESER525
EGLY523
EHIS363

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP419
BSER525
BHIS363
BGLY526

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASP419
ESER525
EHIS363
EGLY526

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP419
BSER525
BHIS363

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASP419
ESER525
EHIS363

242500

PDB entries from 2025-10-01

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