8ZGE
Human lysine O-link glycosylation complex, LH3/ColGalT1 tetramer with bound UDP-galactose
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0008475 | molecular_function | procollagen-lysine 5-dioxygenase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0031418 | molecular_function | L-ascorbic acid binding |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0008475 | molecular_function | procollagen-lysine 5-dioxygenase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0031418 | molecular_function | L-ascorbic acid binding |
| U | 0005788 | cellular_component | endoplasmic reticulum lumen |
| U | 0016020 | cellular_component | membrane |
| U | 0016740 | molecular_function | transferase activity |
| U | 0016757 | molecular_function | glycosyltransferase activity |
| U | 0030199 | biological_process | collagen fibril organization |
| U | 0050211 | molecular_function | procollagen galactosyltransferase activity |
| U | 0180062 | biological_process | protein O-linked glycosylation via galactose |
| U | 1904028 | biological_process | positive regulation of collagen fibril organization |
| V | 0005788 | cellular_component | endoplasmic reticulum lumen |
| V | 0016020 | cellular_component | membrane |
| V | 0016740 | molecular_function | transferase activity |
| V | 0016757 | molecular_function | glycosyltransferase activity |
| V | 0030199 | biological_process | collagen fibril organization |
| V | 0050211 | molecular_function | procollagen galactosyltransferase activity |
| V | 0180062 | biological_process | protein O-linked glycosylation via galactose |
| V | 1904028 | biological_process | positive regulation of collagen fibril organization |
Functional Information from PROSITE/UniProt
| site_id | PS01325 |
| Number of Residues | 8 |
| Details | LYS_HYDROXYLASE Lysyl hydroxylase signature. PHHDSSTF |
| Chain | Residue | Details |
| A | PRO666-PHE673 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 182 |
| Details | Domain: {"description":"Fe2OG dioxygenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 450 |
| Details | Region: {"description":"Accessory region","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 86 |
| Details | Region: {"description":"Important for dimerization","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| 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_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FXY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| 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 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 68 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | Motif: {"description":"Endoplasmic reticulum retention motif","evidences":[{"source":"PubMed","id":"20470363","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 36 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
