2SPT

DIFFERENCES IN THE METAL ION STRUCTURE BETWEEN SR-AND CA-PROTHROMBIN FRAGMENT 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0005576	cellular_component	extracellular region

Functional Information from PROSITE/UniProt

site_id	PS00011
Number of Residues	26
Details	GLA_1 Vitamin K-dependent carboxylation domain. EclEEpCsreeafEaleslsatda.FW

Chain	Residue	Details
A	CGU17-TRP42

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site_id	PS00021
Number of Residues	14
Details	KRINGLE_1 Kringle domain signature. FCRNpdgsitgpWC

Chain	Residue	Details
A	PHE114-CYS127

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Glycosylation: {"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."]}}]}

Chain

Residue

Details

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