9E6V
Cryo-EM structure of Saccharomyces cerevisiae Pmt4-Ccw5 complex
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000030 | molecular_function | mannosyltransferase activity |
| A | 0004169 | molecular_function | dolichyl-phosphate-mannose-protein mannosyltransferase activity |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006486 | biological_process | obsolete protein glycosylation |
| A | 0006493 | biological_process | protein O-linked glycosylation |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0035269 | biological_process | protein O-linked glycosylation via mannose |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0097586 | cellular_component | dolichyl-phosphate-mannose-protein mannosyltransferase Pmt4p homodimer complex |
| A | 1900101 | biological_process | regulation of endoplasmic reticulum unfolded protein response |
| B | 0000030 | molecular_function | mannosyltransferase activity |
| B | 0004169 | molecular_function | dolichyl-phosphate-mannose-protein mannosyltransferase activity |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006486 | biological_process | obsolete protein glycosylation |
| B | 0006493 | biological_process | protein O-linked glycosylation |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0035269 | biological_process | protein O-linked glycosylation via mannose |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0097586 | cellular_component | dolichyl-phosphate-mannose-protein mannosyltransferase Pmt4p homodimer complex |
| B | 1900101 | biological_process | regulation of endoplasmic reticulum unfolded protein response |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 400 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 824 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 154 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 120 |
| Details | Domain: {"description":"MIR 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00131","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 118 |
| Details | Domain: {"description":"MIR 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00131","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 114 |
| Details | Domain: {"description":"MIR 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00131","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"O-linked (Man) threonine","evidences":[{"source":"PubMed","id":"12776183","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"O-linked (Man) serine","evidences":[{"source":"PubMed","id":"12776183","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
