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1FF7

THE FIRST EGF-LIKE DOMAIN FROM HUMAN BLOOD COAGULATION FVII (FUCOSYLATED AT SER-60), NMR, 20 STRUCTURES

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDqlqsYiCfC
ChainResidueDetails
ACYS61-CYS72

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CfClpAfeGRnC
ChainResidueDetails
ACYS70-CYS81

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCassp..........Cqnggs..CkDqlqsYiC
ChainResidueDetails
AASP46-CYS70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsDomain: {"description":"EGF-like 1; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Important for S-112 for O-xylosylation"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"3264725","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Xyl...) serine; alternate","evidences":[{"source":"PubMed","id":"1904059","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2129367","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21949356","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2511201","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Fuc) serine","featureId":"CAR_000180","evidences":[{"source":"PubMed","id":"1904059","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9023546","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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