Research workbench
Structure of the dead domain of human eukaryotic initiation factor 4A, EIF4A
Analyse Structure of the dead domain of human eukaryotic initiation factor 4A, EIF4A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G9N
- Type
- protein
- Length
- 431 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eukaryotic initiation factor 4A-I
- EC
- 3.6.1.-
- UniProt
- P60842
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eukaryotic initiation factor 4A-I (EC 3.6.1.-) | protein | 216 | 40% helix, 14% strand | P60842 |
| B | Eukaryotic initiation factor 4A-I (EC 3.6.1.-) | protein | 215 | 44% helix, 14% strand | P60842 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 335 | 0.65 | 0.80 | 44 | empty |
| 2 | 51 | 0.38 | 0.81 | 19 | empty |
| 3 | 56 | 0.35 | 0.78 | 14 | empty |
| 4 | 52 | 0.28 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 826 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 27 modified (methylation).
Compared structures
- 2G9N · Structure of the DEAD domain of Human eukaryotic initiation factor 4A, eIF4A · the same entry in another collection · chain A against A, TM-score 1.00
- P60842 · AlphaFold monomer V2.0 prediction for eukaryotic initiation factor 4A-I (P60842) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P60842
- Elsewhere: RCSB PDB 2G9N · PDBe 2G9N · UniProt P60842
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