3DMK
Crystal structure of Down Syndrome Cell Adhesion Molecule (DSCAM) isoform 1.30.30, N-terminal eight Ig domains
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007155 | biological_process | cell adhesion |
| A | 0007411 | biological_process | axon guidance |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007155 | biological_process | cell adhesion |
| B | 0007411 | biological_process | axon guidance |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0007155 | biological_process | cell adhesion |
| C | 0007411 | biological_process | axon guidance |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 285 |
| Details | Domain: {"description":"Ig-like C2-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 276 |
| Details | Domain: {"description":"Ig-like C2-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 237 |
| Details | Domain: {"description":"Ig-like C2-type 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 282 |
| Details | Domain: {"description":"Ig-like C2-type 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 258 |
| Details | Domain: {"description":"Ig-like C2-type 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 92 |
| Details | Domain: {"description":"Ig-like C2-type 8","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17721508","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18805093","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27386517","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V5M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V5R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DMK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XHQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18805093","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3DMK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18805093","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3DMK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 9 |
| Details | Binding site: {"description":"ligand shared between homodimeric partners","evidences":[{"source":"PubMed","id":"27386517","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4XB8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
