5LEV
Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) (V264G mutant)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003975 | molecular_function | UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity |
| A | 0003976 | molecular_function | UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0006486 | biological_process | protein glycosylation |
| A | 0006487 | biological_process | protein N-linked glycosylation |
| A | 0006488 | biological_process | dolichol-linked oligosaccharide biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue PC1 A 501 |
| Chain | Residue |
| A | SER204 |
| A | LEU239 |
| A | TRP243 |
| A | ARG377 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 27 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 1","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 114 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 2","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 3","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 4","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 5","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 6","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 5 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 7","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 8","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 9","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 10","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30388443","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BW5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BW6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BW5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30388443","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BW6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
