Research workbench
Electron cryo-microscopy of the eukaryotic translation initiation factor 2B bound to eukaryotic translation initiation factor 2 from homo sapiens
Analyse Electron cryo-microscopy of the eukaryotic translation initiation factor 2B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6O9Z
- Type
- protein
- Length
- 3,605 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Translation initiation factor eif-2B subunit epsilon; Translation initiation factor…
- UniProt
- Q13144, P49770, Q9UI10, Q14232, Q9NR50, P05198
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 7 distinct chains · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Translation initiation factor eif-2B subunit epsilon | protein | 426 | 20% helix, 25% strand | Q13144 |
| C | Translation initiation factor eif-2B subunit beta | protein | 317 | 49% helix, 14% strand | P49770 |
| D | Translation initiation factor eif-2B subunit beta | protein | 318 | 47% helix, 14% strand | P49770 |
| E, F | Translation initiation factor eif-2B subunit delta | protein | 353 | 42% helix, 14% strand | Q9UI10 |
| G, H | Translation initiation factor eif-2B subunit alpha | protein | 290 | 48% helix, 14% strand | Q14232 |
| I, J | Translation initiation factor eif-2B subunit gamma | protein | 240 | 27% helix, 22% strand | Q9NR50 |
| L, M | Eukaryotic translation initiation factor 2 subunit 1 | protein | 176 | 45% helix, 20% strand | P05198 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1094 | 0.86 | 0.87 | 123 | empty |
| 2 | 900 | 0.85 | 0.87 | 108 | empty |
| 3 | 913 | 0.76 | 0.79 | 98 | empty |
| 4 | 910 | 0.76 | 0.79 | 88 | empty |
| 5 | 775 | 0.75 | 0.80 | 103 | empty |
Interfaces
26 interfaces between chains.
- D–E · 2119 Ų buried · 17 hydrogen bonds · protein-protein
- C–F · 2105 Ų buried · 18 hydrogen bonds · protein-protein
- G–H · 1322 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 1247 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 1228 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 6O9Z · Electron cryo-microscopy of the eukaryotic translation initiation factor 2B bound to… · the same entry in another collection · chain M against M, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q13144
- Every structure of UniProt P49770
- Every structure of UniProt Q9UI10
- Every structure of UniProt Q14232
- Every structure of UniProt Q9NR50
- Every structure of UniProt P05198
- Elsewhere: RCSB PDB 6O9Z · PDBe 6O9Z · UniProt Q13144 · UniProt P49770 · UniProt Q9UI10 · UniProt Q14232 · UniProt Q9NR50 · UniProt P05198
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