4FMF
Crystal structure of human nectin-1 full ectodomain (D1-D3)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005911 | cellular_component | cell-cell junction |
| A | 0007155 | biological_process | cell adhesion |
| A | 0016021 | cellular_component | integral component of membrane |
| A | 0019062 | biological_process | virion attachment to host cell |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0045202 | cellular_component | synapse |
| A | 0050839 | molecular_function | cell adhesion molecule binding |
| A | 0051963 | biological_process | regulation of synapse assembly |
| B | 0005911 | cellular_component | cell-cell junction |
| B | 0007155 | biological_process | cell adhesion |
| B | 0016021 | cellular_component | integral component of membrane |
| B | 0019062 | biological_process | virion attachment to host cell |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0045202 | cellular_component | synapse |
| B | 0050839 | molecular_function | cell adhesion molecule binding |
| B | 0051963 | biological_process | regulation of synapse assembly |
| C | 0005911 | cellular_component | cell-cell junction |
| C | 0007155 | biological_process | cell adhesion |
| C | 0016021 | cellular_component | integral component of membrane |
| C | 0019062 | biological_process | virion attachment to host cell |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0045202 | cellular_component | synapse |
| C | 0050839 | molecular_function | cell adhesion molecule binding |
| C | 0051963 | biological_process | regulation of synapse assembly |
| D | 0005911 | cellular_component | cell-cell junction |
| D | 0007155 | biological_process | cell adhesion |
| D | 0016021 | cellular_component | integral component of membrane |
| D | 0019062 | biological_process | virion attachment to host cell |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0045202 | cellular_component | synapse |
| D | 0050839 | molecular_function | cell adhesion molecule binding |
| D | 0051963 | biological_process | regulation of synapse assembly |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 356 |
| Details | Domain: {"description":"Ig-like C2-type 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 348 |
| Details | Domain: {"description":"Ig-like C2-type 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 68 |
| Details | Region: {"description":"Interaction with FGFR","evidences":[{"source":"UniProtKB","id":"Q9JKF6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21980294","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21980294","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22902367","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
