6TE3
Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Fe2+, Mn2+, UDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005791 | cellular_component | rough endoplasmic reticulum |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005802 | cellular_component | trans-Golgi network |
| A | 0008475 | molecular_function | procollagen-lysine 5-dioxygenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0030199 | biological_process | collagen fibril organization |
| A | 0031012 | cellular_component | extracellular matrix |
| A | 0031418 | molecular_function | L-ascorbic acid binding |
| A | 0032964 | biological_process | collagen biosynthetic process |
| A | 0033823 | molecular_function | procollagen glucosyltransferase activity |
| A | 0036094 | molecular_function | small molecule binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046947 | biological_process | hydroxylysine biosynthetic process |
| A | 0050211 | molecular_function | procollagen galactosyltransferase activity |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0180062 | biological_process | protein O-linked glycosylation via galactose |
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 | 91 |
| 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 | 225 |
| Details | Region: {"description":"Accessory region","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 43 |
| 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 | 14 |
| 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 | 3 |
| 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 | 2 |
| 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 |
