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7OCI

Cryo-EM structure of yeast Ost6p containing oligosaccharyltransferase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0006486biological_processprotein glycosylation
A0016020cellular_componentmembrane
B0003674molecular_functionmolecular_function
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006486biological_processprotein glycosylation
B0006487biological_processprotein N-linked glycosylation
B0008250cellular_componentoligosaccharyltransferase complex
B0016020cellular_componentmembrane
D0005515molecular_functionprotein binding
D0005739cellular_componentmitochondrion
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0006486biological_processprotein glycosylation
D0006487biological_processprotein N-linked glycosylation
D0008250cellular_componentoligosaccharyltransferase complex
D0016020cellular_componentmembrane
D0030674molecular_functionprotein-macromolecule adaptor activity
E0005198molecular_functionstructural molecule activity
E0005783cellular_componentendoplasmic reticulum
E0005789cellular_componentendoplasmic reticulum membrane
E0006486biological_processprotein glycosylation
E0006487biological_processprotein N-linked glycosylation
E0008250cellular_componentoligosaccharyltransferase complex
E0016020cellular_componentmembrane
E0034998cellular_componentobsolete oligosaccharyltransferase I complex
F0004576molecular_functionoligosaccharyl transferase activity
F0004579molecular_functiondolichyl-diphosphooligosaccharide-protein glycotransferase activity
F0005515molecular_functionprotein binding
F0005783cellular_componentendoplasmic reticulum
F0005789cellular_componentendoplasmic reticulum membrane
F0006486biological_processprotein glycosylation
F0006487biological_processprotein N-linked glycosylation
F0008250cellular_componentoligosaccharyltransferase complex
F0016020cellular_componentmembrane
F0016757molecular_functionglycosyltransferase activity
F0018279biological_processprotein N-linked glycosylation via asparagine
F0043687biological_processpost-translational protein modification
F0046872molecular_functionmetal ion binding
G0005789cellular_componentendoplasmic reticulum membrane
G0018279biological_processprotein N-linked glycosylation via asparagine
H0006487biological_processprotein N-linked glycosylation
H0008250cellular_componentoligosaccharyltransferase complex
H0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues174
DetailsTOPO_DOM: Lumenal => ECO:0000305|PubMed:29301962
ChainResidueDetails
HTYR19-PRO194
FLYS138-ASP139
FGLY189-SER190
FMET228-SER232
FGLY287-VAL300
FLEU379-GLU384
FTYR428-LYS441

site_idSWS_FT_FI2
Number of Residues60
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:29301962
ChainResidueDetails
HILE195-LEU215
FHIS385-VAL401
FMET406-ILE427
FPRO442-PHE464
HVAL229-ALA249
HLEU253-LEU273
FALA169-THR188
FILE191-VAL205
FTYR211-LEU227
FSER233-PHE258
FMET267-LYS286
FTRP356-PHE378

site_idSWS_FT_FI3
Number of Residues24
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
HASN216-GLY228
HTHR274-ILE286
FSER206-GLY210
FLEU259-HIS266
FALA323-SER355
FMET402-LEU405
FHIS465-VAL718

site_idSWS_FT_FI4
Number of Residues2
DetailsTOPO_DOM: Lumenal => ECO:0000305
ChainResidueDetails
HARG250-TYR252
GASN332
AASN217

site_idSWS_FT_FI5
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:B9KDD4
ChainResidueDetails
FASP47
FASP166
FGLU168
FARG404
FTYR521

site_idSWS_FT_FI6
Number of Residues3
DetailsSITE: Interacts with target acceptor peptide in protein substrate => ECO:0000250|UniProtKB:B9KDD4
ChainResidueDetails
FASP47
FGLU350
FLYS586

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000250|UniProtKB:B9KDD4
ChainResidueDetails
FARG159

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
FASN60
FASN535

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:29301962
ChainResidueDetails
FASN539

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PDB entries from 2024-10-16

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