6P2R
Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor
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 | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006493 | biological_process | protein O-linked glycosylation |
| A | 0009272 | biological_process | fungal-type cell wall biogenesis |
| A | 0016020 | cellular_component | membrane |
| A | 0031502 | cellular_component | dolichyl-phosphate-mannose-protein mannosyltransferase complex |
| A | 0032527 | biological_process | protein exit from endoplasmic reticulum |
| A | 0035269 | biological_process | protein O-linked glycosylation via mannose |
| A | 0036503 | biological_process | ERAD pathway |
| A | 0097582 | cellular_component | dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex |
| A | 0097583 | cellular_component | dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt3p dimer 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 | 0005515 | molecular_function | protein binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006493 | biological_process | protein O-linked glycosylation |
| B | 0009272 | biological_process | fungal-type cell wall biogenesis |
| B | 0016020 | cellular_component | membrane |
| B | 0031502 | cellular_component | dolichyl-phosphate-mannose-protein mannosyltransferase complex |
| B | 0032527 | biological_process | protein exit from endoplasmic reticulum |
| B | 0035269 | biological_process | protein O-linked glycosylation via mannose |
| B | 0036503 | biological_process | ERAD pathway |
| B | 0097582 | cellular_component | dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex |
| B | 0097584 | cellular_component | dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt2p dimer 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 | 142 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"10085156","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 97 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"10085156","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 116 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"10085156","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 109 |
| 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 | 116 |
| 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 | 113 |
| 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 | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 180 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 119 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 53 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
