9ZNN
Cryo-EM structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) in complex with APPB
This is a non-PDB format compatible entry.
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 | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0006487 | biological_process | protein N-linked glycosylation |
| A | 0006488 | biological_process | dolichol-linked oligosaccharide biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| B | 0003975 | molecular_function | UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity |
| B | 0003976 | molecular_function | UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0006487 | biological_process | protein N-linked glycosylation |
| B | 0006488 | biological_process | dolichol-linked oligosaccharide biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 54 |
| 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 | 228 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 38 |
| 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 | 52 |
| 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 | 42 |
| 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 | 54 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 38 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 5","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 6","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 46 |
| 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 | 36 |
| 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 | 42 |
| 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 | 48 |
| 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 | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30388443","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| 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 | 4 |
| 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 | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30388443","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| 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 | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
