3MTR
Crystal structure of the Ig5-FN1 tandem of human NCAM
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1 |
| Chain | Residue |
| B | TYR511 |
| B | TYR511 |
| B | SER512 |
| B | SER512 |
| B | SER513 |
| B | SER513 |
| B | THR514 |
| B | THR514 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 170 |
| Details | Domain: {"description":"Ig-like C2-type 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9774483","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9774483","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 99 |
| Details | Domain: {"description":"Fibronectin type-III 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
