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6C26

The Cryo-EM structure of a eukaryotic oligosaccharyl transferase complex

Functional Information from GO Data
ChainGOidnamespacecontents
10006486biological_processprotein glycosylation
10016020cellular_componentmembrane
20003674molecular_functionmolecular_function
20005515molecular_functionprotein binding
20005783cellular_componentendoplasmic reticulum
20005789cellular_componentendoplasmic reticulum membrane
20006486biological_processprotein glycosylation
20006487biological_processprotein N-linked glycosylation
20008250cellular_componentoligosaccharyltransferase complex
20016020cellular_componentmembrane
40005515molecular_functionprotein binding
40005739cellular_componentmitochondrion
40005783cellular_componentendoplasmic reticulum
40005789cellular_componentendoplasmic reticulum membrane
40006486biological_processprotein glycosylation
40006487biological_processprotein N-linked glycosylation
40008250cellular_componentoligosaccharyltransferase complex
40016020cellular_componentmembrane
40030674molecular_functionprotein-macromolecule adaptor activity
50005198molecular_functionstructural molecule activity
50005783cellular_componentendoplasmic reticulum
50005789cellular_componentendoplasmic reticulum membrane
50006486biological_processprotein glycosylation
50006487biological_processprotein N-linked glycosylation
50008250cellular_componentoligosaccharyltransferase complex
50016020cellular_componentmembrane
50034998cellular_componentobsolete oligosaccharyltransferase I complex
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
B0005789cellular_componentendoplasmic reticulum membrane
B0018279biological_processprotein N-linked glycosylation via asparagine
C0006487biological_processprotein N-linked glycosylation
C0008250cellular_componentoligosaccharyltransferase complex
C0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues369
DetailsTOPO_DOM: Lumenal => ECO:0000305|PubMed:29301962
ChainResidueDetails
BSER24-TRP393
3GLN239-MET273
3THR328-LYS350
AMET228-SER232
AGLY287-VAL300
ALEU379-GLU384
ATYR428-LYS441

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:29301962
ChainResidueDetails
BVAL394-VAL414
AHIS385-VAL401
AMET406-ILE427
APRO442-PHE464
CVAL229-ALA249
CLEU253-LEU273
AALA169-THR188
AILE191-VAL205
ATYR211-LEU227
ASER233-PHE258
AMET267-LYS286
ATRP356-PHE378

site_idSWS_FT_FI3
Number of Residues15
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:1724755
ChainResidueDetails
BTHR415-ASN430
CTHR274-ILE286
ASER206-GLY210
ALEU259-HIS266
AALA323-SER355
AMET402-LEU405
AHIS465-VAL718

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:29301962
ChainResidueDetails
BASN60
BASN332
3PHE307-LEU327

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:29301962
ChainResidueDetails
1ASN336
1ASN400
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 2024-10-16

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