Research workbench
EIF2B:EIF2 complex, phosphorylated on EIF2 alpha serine 52.
Analyse EIF2B:EIF2 complex, phosphorylated on EIF2 alpha serine 52. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6I3M
- Type
- protein
- Length
- 4,682 residues
- Chains
- 16
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Translation initiation factor eif-2B subunit alpha; Translation initiation factor eif-2B…
- UniProt
- P14741, P12754, P32502, P32501, P09032, P20459, P09064, P32481
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · 8 distinct chains · 29% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Translation initiation factor eif-2B subunit alpha | protein | 305 | 36% helix, 9% strand | P14741 |
| C, D | Translation initiation factor eif-2B subunit delta | protein | 342 | 41% helix, 11% strand | P12754 |
| E, F | Translation initiation factor eif-2B subunit beta | protein | 354 | 42% helix, 9% strand | P32502 |
| G, H | Translation initiation factor eif-2B subunit epsilon | protein | 410 | 15% helix, 22% strand | P32501 |
| I, J | Translation initiation factor eif-2B subunit gamma | protein | 268 | 17% helix, 9% strand | P09032 |
| K, L | Eukaryotic translation initiation factor 2 subunit alpha | protein | 249 | 41% helix, 16% strand | P20459 |
| M, N | Eukaryotic translation initiation factor 2 subunit beta | protein | 17 | 53% helix, 0% strand | P09064 |
| O, P | Eukaryotic translation initiation factor 2 subunit gamma | protein | 396 | 13% helix, 40% strand | P32481 |
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 | 797 | 0.89 | 0.92 | 120 | empty |
| 2 | 864 | 0.83 | 0.85 | 108 | empty |
| 3 | 324 | 0.80 | 0.90 | 46 | empty |
| 4 | 329 | 0.80 | 0.90 | 47 | empty |
| 5 | 555 | 0.78 | 0.84 | 80 | empty |
Interfaces
33 interfaces between chains.
- D–F · 2422 Ų buried · 22 hydrogen bonds · protein-protein
- C–E · 2386 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 2045 Ų buried · 12 hydrogen bonds · protein-protein
- G–F · 1343 Ų buried · 10 hydrogen bonds · protein-protein
- E–H · 1341 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 6I3M · eIF2B:eIF2 complex, phosphorylated on eIF2 alpha serine 52. · the same entry in another collection · chain K against K, 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 P14741
- Every structure of UniProt P12754
- Every structure of UniProt P32502
- Every structure of UniProt P32501
- Every structure of UniProt P09032
- Every structure of UniProt P20459
- Every structure of UniProt P09064
- Every structure of UniProt P32481
- Elsewhere: RCSB PDB 6I3M · PDBe 6I3M · UniProt P14741 · UniProt P12754 · UniProt P32502 · UniProt P32501 · UniProt P09032 · UniProt P20459 · UniProt P09064 · UniProt P32481
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