6EZN
Cryo-EM structure of the yeast oligosaccharyltransferase (OST) complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006486 | biological_process | protein glycosylation |
| A | 0016020 | cellular_component | membrane |
| B | 0003674 | molecular_function | molecular_function |
| B | 0005515 | molecular_function | protein binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006486 | biological_process | protein glycosylation |
| B | 0006487 | biological_process | protein N-linked glycosylation |
| B | 0008250 | cellular_component | oligosaccharyltransferase complex |
| B | 0016020 | cellular_component | membrane |
| D | 0005515 | molecular_function | protein binding |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005789 | cellular_component | endoplasmic reticulum membrane |
| D | 0006486 | biological_process | protein glycosylation |
| D | 0006487 | biological_process | protein N-linked glycosylation |
| D | 0008250 | cellular_component | oligosaccharyltransferase complex |
| D | 0016020 | cellular_component | membrane |
| D | 0030674 | molecular_function | protein-macromolecule adaptor activity |
| E | 0005198 | molecular_function | structural molecule activity |
| E | 0005783 | cellular_component | endoplasmic reticulum |
| E | 0005789 | cellular_component | endoplasmic reticulum membrane |
| E | 0006486 | biological_process | protein glycosylation |
| E | 0006487 | biological_process | protein N-linked glycosylation |
| E | 0008250 | cellular_component | oligosaccharyltransferase complex |
| E | 0016020 | cellular_component | membrane |
| F | 0004576 | molecular_function | oligosaccharyl transferase activity |
| F | 0004579 | molecular_function | dolichyl-diphosphooligosaccharide-protein glycotransferase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005783 | cellular_component | endoplasmic reticulum |
| F | 0005789 | cellular_component | endoplasmic reticulum membrane |
| F | 0006486 | biological_process | protein glycosylation |
| F | 0006487 | biological_process | protein N-linked glycosylation |
| F | 0008250 | cellular_component | oligosaccharyltransferase complex |
| F | 0016020 | cellular_component | membrane |
| F | 0016740 | molecular_function | transferase activity |
| F | 0016757 | molecular_function | glycosyltransferase activity |
| F | 0018279 | biological_process | protein N-linked glycosylation via asparagine |
| F | 0043687 | biological_process | post-translational protein modification |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0005789 | cellular_component | endoplasmic reticulum membrane |
| G | 0018279 | biological_process | protein N-linked glycosylation via asparagine |
| H | 0008250 | cellular_component | oligosaccharyltransferase complex |
| H | 0016020 | cellular_component | membrane |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 260 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 23 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 23 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"12810948","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"12810948","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 33 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 230 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"29466327","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 111 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29466327","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 11 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29466327","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Region: {"description":"Interacts with target acceptor peptide in protein substrate","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 24 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Motif: {"description":"DXD motif 1","evidences":[{"source":"UniProtKB","id":"Q5HTX9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Motif: {"description":"DXD motif 2","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 4 |
| Details | Motif: {"description":"WWDYG motif","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 7 |
| Details | Motif: {"description":"DK motif","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 2 |
| Details | Site: {"description":"Interacts with target acceptor peptide in protein substrate","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 2 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
