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The cryo-EM structure of a eukaryotic oligosaccharyl transferase complex

Analyse The cryo-EM structure of a eukaryotic oligosaccharyl transferase complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6C26
Type
protein
Length
2,077 residues
Chains
8
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3…
EC
2.4.99.18
UniProt
P39007, P41543, Q92316, Q99380, P46964, P48439, Q02795, P33767
Ligands
EGY, BMA, NAG
Pockets
20 · best druggability 0.76

Structure

electron microscopy · 8 distinct chains · 36% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3 (EC 2.4.99.18)protein64848% helix, 5% strandP39007
1Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 (EC 2.4.99.18)protein4329% helix, 39% strandP41543
5Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST5 (EC 2.4.99.18)protein8468% helix, 1% strandQ92316
4Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4 (EC 2.4.99.18)protein3482% helix, 0% strandQ99380
2Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2 (EC 2.4.99.18)protein10878% helix, 0% strandP46964
3Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3 (EC 2.4.99.18)protein12664% helix, 0% strandP48439
CDolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit SWP1 (EC 2.4.99.18)protein24830% helix, 14% strandQ02795
BDolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1 (EC 2.4.99.18)protein39716% helix, 29% strandP33767

Ligands and binding sites

  • EGY · (4R,7R)-4-hydroxy-N,N,N-trimethyl-4,9-dioxo-7-[(undecanoyloxy)methyl]-3,5,8-trioxa-4lambda~5~-phosphadocosan-1-aminium · ligand · 8 copies · chains A, 1, C, 2, 5, 4, 3, B
  • BMA · beta-D-mannopyranose · sugar · 6 copies · chains B, C
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, B, 1

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110450.760.7882EGY
23570.740.8545empty
31980.730.8936empty
4710.720.9623empty
5650.680.9525empty

Interfaces

14 interfaces between chains.

  • C–B · 2630 Ų buried · 8 hydrogen bonds · protein-protein
  • A–3 · 2377 Ų buried · 4 hydrogen bonds · protein-protein
  • 1–5 · 1799 Ų buried · 6 hydrogen bonds · protein-protein
  • A–4 · 1615 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 1457 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 glycan (N-glycosylation).

Compared structures

  • 6C26 · The Cryo-EM structure of a eukaryotic oligosaccharyl transferase complex · the same entry in another collection · chain B against B, TM-score 1.00
  • P41543 · AlphaFold monomer V2.0 prediction for dolichyl- diphosphooligosaccharide--protein… · a predicted model of the same protein · chain 1 against A, TM-score 0.96
  • P46964 · AlphaFold monomer V2.0 prediction for dolichyl- diphosphooligosaccharide--protein… · a predicted model of the same protein · chain 2 against A, TM-score 0.94
  • P39007 · AlphaFold monomer V2.0 prediction for dolichyl- diphosphooligosaccharide--protein… · a predicted model of the same protein · chain A against A, TM-score 0.93
  • P33767 · AlphaFold monomer V2.0 prediction for dolichyl- diphosphooligosaccharide--protein… · a predicted model of the same protein · chain B against A, TM-score 0.93

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