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6P25

Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor and a peptide acceptor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000030molecular_functionmannosyltransferase activity
A0004169molecular_functiondolichyl-phosphate-mannose-protein mannosyltransferase activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006486biological_processobsolete protein glycosylation
A0006493biological_processprotein O-linked glycosylation
A0009272biological_processfungal-type cell wall biogenesis
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0031502cellular_componentdolichyl-phosphate-mannose-protein mannosyltransferase complex
A0032527biological_processprotein exit from endoplasmic reticulum
A0035269biological_processprotein O-linked glycosylation via mannose
A0036503biological_processERAD pathway
A0097582cellular_componentdolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex
A0097583cellular_componentdolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt3p dimer complex
A1900101biological_processregulation of endoplasmic reticulum unfolded protein response
B0000030molecular_functionmannosyltransferase activity
B0004169molecular_functiondolichyl-phosphate-mannose-protein mannosyltransferase activity
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006486biological_processobsolete protein glycosylation
B0006493biological_processprotein O-linked glycosylation
B0009272biological_processfungal-type cell wall biogenesis
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0031502cellular_componentdolichyl-phosphate-mannose-protein mannosyltransferase complex
B0032527biological_processprotein exit from endoplasmic reticulum
B0035269biological_processprotein O-linked glycosylation via mannose
B0036503biological_processERAD pathway
B0097582cellular_componentdolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex
B0097584cellular_componentdolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt2p dimer complex
B1900101biological_processregulation of endoplasmic reticulum unfolded protein response
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues142
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"10085156","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues97
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"10085156","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues116
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"10085156","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues109
DetailsDomain: {"description":"MIR 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00131","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues116
DetailsDomain: {"description":"MIR 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00131","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues113
DetailsDomain: {"description":"MIR 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00131","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues180
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues119
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues53
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-01-14

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