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 |
