1E88
Solution structure of 6F11F22F2, a compact three-module fragment of the gelatin-binding domain of human fibronectin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
Functional Information from PROSITE/UniProt
| site_id | PS00023 |
| Number of Residues | 42 |
| Details | FN2_1 Fibronectin type-II collagen-binding domain signature. CvlPFtYngrtfysCttegrqdghlWCsttsNYeqdqkYsFC |
| Chain | Residue | Details |
| A | CYS56-CYS97 | |
| A | CYS116-CYS157 |
| site_id | PS01253 |
| Number of Residues | 35 |
| Details | FN1_1 Fibronectin type-I domain signature. Cvtdsgvv.YsvgmqWlKtqgnkqml..CtClgngvs...C |
| Chain | Residue | Details |
| A | CYS4-CYS38 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 39 |
| Details | Domain: {"description":"Fibronectin type-I 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00478","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | Domain: {"description":"Fibronectin type-II 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00478","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 48 |
| Details | Domain: {"description":"Fibronectin type-II 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00478","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11285216","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16037490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
