5CVB
Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a1a1a1 of type I collagen
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 101 |
| Chain | Residue |
| A | GLU54 |
| A | HIS55 |
| B | VAL45 |
| C | GLN19 |
| C | ALA20 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue GOL C 101 |
| Chain | Residue |
| C | GLN58 |
| C | HOH202 |
| C | HOH206 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL F 101 |
| Chain | Residue |
| E | GLN55 |
| E | GLU58 |
| F | SER53 |
| F | ALA57 |
| A | ASP41 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL F 102 |
| Chain | Residue |
| A | THR40 |
| A | ASP41 |
| C | ARG43 |
| E | GLN55 |
| F | GLY49 |
| F | HOH215 |
| F | HOH216 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL F 103 |
| Chain | Residue |
| C | GLU46 |
| E | ALA60 |
| F | ALA60 |
| F | ARG64 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | Modified residue: {"description":"4-hydroxyproline","evidences":[{"source":"UniProtKB","id":"P02457","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 94 |
| Details | Compositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
