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2PF1

STRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REFINED AT 2.25 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
Functional Information from PROSITE/UniProt
site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EclEEpCsreeafEaleslsatda.FW
ChainResidueDetails
ACGU17-TRP42

site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. FCRNpdgsitgpWC
ChainResidueDetails
APHE114-CYS127

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1547238","evidenceCode":"ECO:0000269"},{"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

245663

PDB entries from 2025-12-03

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