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8AGE

Structure of yeast oligosaccharylransferase complex with acceptor peptide bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004576molecular_functionoligosaccharyl transferase activity
A0004579molecular_functiondolichyl-diphosphooligosaccharide-protein glycotransferase activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006486biological_processprotein glycosylation
A0006487biological_processprotein N-linked glycosylation
A0008250cellular_componentoligosaccharyltransferase complex
A0016020cellular_componentmembrane
A0016757molecular_functionglycosyltransferase activity
A0018279biological_processprotein N-linked glycosylation via asparagine
A0043687biological_processpost-translational protein modification
A0046872molecular_functionmetal ion binding
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006486biological_processprotein glycosylation
B0006487biological_processprotein N-linked glycosylation
B0008250cellular_componentoligosaccharyltransferase complex
B0016020cellular_componentmembrane
B0030674molecular_functionprotein-macromolecule adaptor activity
C0005198molecular_functionstructural molecule activity
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0006486biological_processprotein glycosylation
C0006487biological_processprotein N-linked glycosylation
C0008250cellular_componentoligosaccharyltransferase complex
C0016020cellular_componentmembrane
C0034998cellular_componentoligosaccharyltransferase I complex
D0003674molecular_functionmolecular_function
D0005515molecular_functionprotein binding
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0006486biological_processprotein glycosylation
D0006487biological_processprotein N-linked glycosylation
D0008250cellular_componentoligosaccharyltransferase complex
D0016020cellular_componentmembrane
E0006486biological_processprotein glycosylation
E0016020cellular_componentmembrane
F0006487biological_processprotein N-linked glycosylation
F0008250cellular_componentoligosaccharyltransferase complex
F0016020cellular_componentmembrane
G0005789cellular_componentendoplasmic reticulum membrane
G0018279biological_processprotein N-linked glycosylation via asparagine
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues215
DetailsTOPO_DOM: Lumenal => ECO:0000305
ChainResidueDetails
HMET23-LEU182
HGLN239-MET273
HTHR328-LYS350
AMET228-SER232
AGLY287-VAL300
ALEU379-GLU384
ATYR428-LYS441

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
HPRO183-PHE203
AHIS385-VAL401
AMET406-ILE427
APRO442-PHE464
FVAL226-ALA246
FLEU250-LEU270
AALA169-THR188
AILE191-VAL205
ATYR211-LEU227
ASER233-PHE258
AMET267-LYS286
ATRP356-PHE378

site_idSWS_FT_FI3
Number of Residues24
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
HLYS204-ARG217
HARG295-TYR306
ASER206-GLY210
ALEU259-HIS266
AALA323-SER355
AMET402-LEU405
AHIS465-VAL718

site_idSWS_FT_FI4
Number of Residues60
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:29301962
ChainResidueDetails
HILE218-ASN238
HVAL274-LEU294
HPHE307-LEU327

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:29301962
ChainResidueDetails
EASN336
EASN400
AGLU168
AARG404
ATYR521

site_idSWS_FT_FI6
Number of Residues3
DetailsSITE: Interacts with target acceptor peptide in protein substrate => ECO:0000250|UniProtKB:B9KDD4
ChainResidueDetails
AASP47
AGLU350
ALYS586

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000250|UniProtKB:B9KDD4
ChainResidueDetails
AARG159

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN60
AASN535

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:29301962
ChainResidueDetails
AASN539

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PDB entries from 2024-07-17

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