Research workbench
The eukaryotic translation initiation factor 2B from homo sapiens with a H160D mutation in the beta subunit
Analyse The eukaryotic translation initiation factor 2B from homo sapiens with a H160D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TRJ
- Type
- protein
- Length
- 3,234 residues
- Chains
- 10
- 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
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 5 distinct chains · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Translation initiation factor eif-2B subunit epsilon | protein | 414 | 21% helix, 26% strand | Q13144 |
| D, C | Translation initiation factor eif-2B subunit beta | protein | 329 | 48% helix, 14% strand | P49770 |
| E, F | Translation initiation factor eif-2B subunit delta | protein | 353 | 46% helix, 14% strand | Q9UI10 |
| G, H | Translation initiation factor eif-2B subunit alpha | protein | 285 | 49% helix, 13% strand | Q14232 |
| I, J | Translation initiation factor eif-2B subunit gamma | protein | 236 | 30% helix, 28% strand | Q9NR50 |
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 | 918 | 0.86 | 0.87 | 132 | empty |
| 2 | 557 | 0.82 | 0.88 | 78 | empty |
| 3 | 909 | 0.80 | 0.82 | 103 | empty |
| 4 | 954 | 0.76 | 0.79 | 88 | empty |
| 5 | 331 | 0.74 | 0.86 | 49 | empty |
Interfaces
22 interfaces between chains.
- D–E · 2224 Ų buried · 19 hydrogen bonds · protein-protein
- C–F · 2193 Ų buried · 18 hydrogen bonds · protein-protein
- G–H · 1331 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1208 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 1192 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7TRJ · The eukaryotic translation initiation factor 2B from Homo sapiens with a H160D mutation… · the same entry in another collection · chain J against J, TM-score 1.00
- Q13144 · AlphaFold monomer V2.0 prediction for translation initiation factor eif-2B subunit… · a predicted model of the same protein · chain B against A, TM-score 0.99
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
- Elsewhere: RCSB PDB 7TRJ · PDBe 7TRJ · UniProt Q13144 · UniProt P49770 · UniProt Q9UI10 · UniProt Q14232 · UniProt Q9NR50
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