1F7E
THE FIRST EGF-LIKE DOMAIN FROM HUMAN BLOOD COAGULATION FVII, NMR, 20 STRUCTURES
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDqlqsYiCfC |
Chain | Residue | Details |
A | CYS61-CYS72 |
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CfClpAfeGRnC |
Chain | Residue | Details |
A | CYS70-CYS81 |
site_id | PS01187 |
Number of Residues | 25 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCassp..........Cqnggs..CkDqlqsYiC |
Chain | Residue | Details |
A | ASP46-CYS70 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Important for S-112 for O-xylosylation |
Chain | Residue | Details |
A | ALA75 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420 |
Chain | Residue | Details |
A | GLY47 | |
A | ASP48 | |
A | ALA51 | |
A | ASN57 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:3264725 |
Chain | Residue | Details |
A | LYS85 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (Xyl...) serine; alternate => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:2511201 |
Chain | Residue | Details |
A | PRO74 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (Fuc) serine => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:9023546 |
Chain | Residue | Details |
A | GLU82 |