6WFV
The crystal structure of a collagen galactosylhydroxylysyl glucosyltransferase from human
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue MN A 301 |
| Chain | Residue |
| A | ASP112 |
| A | ASP115 |
| A | HIS253 |
| A | UDP304 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | ASP112 |
| A | ASP115 |
| A | HIS253 |
| A | UDP304 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 303 |
| Chain | Residue |
| A | HOH413 |
| A | HOH450 |
| A | HOH530 |
| A | HOH556 |
| A | HOH563 |
| A | UDP304 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | binding site for residue UDP A 304 |
| Chain | Residue |
| A | VAL44 |
| A | ALA45 |
| A | THR46 |
| A | TRP75 |
| A | LYS89 |
| A | ASP112 |
| A | SER113 |
| A | TYR114 |
| A | ASP115 |
| A | HIS253 |
| A | MN301 |
| A | MG302 |
| A | MG303 |
| A | HOH406 |
| A | HOH413 |
| A | HOH422 |
| A | HOH434 |
| A | HOH465 |
| A | HOH477 |
| A | HOH526 |
| A | HOH530 |
| A | HOH556 |
| A | HOH563 |
| A | HOH567 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue TRS A 305 |
| Chain | Residue |
| A | GLU60 |
| A | ASN63 |
| A | TYR64 |
| A | THR65 |
| A | ASP201 |
| A | LEU204 |
| A | HOH401 |
| A | HOH410 |
| A | HOH552 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FXY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FXY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
