5CTI
Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a2a1a1 of type I collagen (native form)
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 101 |
| Chain | Residue |
| A | GLN42 |
| B | ASN22 |
| B | ILE23 |
| B | ASP46 |
| B | LEU49 |
| B | GLN53 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 101 |
| Chain | Residue |
| C | GLU54 |
| C | GLN55 |
| C | GLN58 |
| A | PHE25 |
| A | HOH106 |
| C | MET51 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 102 |
| Chain | Residue |
| A | PRO26 |
| A | GLY27 |
| A | PHE56 |
| C | GLN55 |
| C | GLN58 |
| C | LEU59 |
| C | HIS62 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 47 |
| Details | Compositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Modified residue: {"description":"4-hydroxyproline","evidences":[{"source":"UniProtKB","id":"P02457","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 59 |
| Details | Region: {"description":"Nonhelical region 3 (NC3)"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
