Research workbench
Autonomous vh domain that interacts with EIF4E at the capped mRNA binding site.
Analyse Autonomous vh domain that interacts with EIF4E at the capped mRNA binding site. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F07
- Type
- protein
- Length
- 316 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eukaryotic translation initiation factor 4E; Vh domain (vh-difcap-01)
- UniProt
- P06730
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eukaryotic translation initiation factor 4E | protein | 188 | 35% helix, 30% strand | P06730 |
| C | Vh domain (vh-difcap-01) | protein | 128 | 5% helix, 48% strand | — |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 297 | 0.57 | 0.77 | 24 | empty |
| 2 | 321 | 0.53 | 0.74 | 39 | empty |
Interfaces
1 interface between chains.
- A–C · 578 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 7F07 · Autonomous VH domain that interacts with eIF4E at the Capped mRNA Binding site. · the same entry in another collection · chain A against A, 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 P06730
- Elsewhere: RCSB PDB 7F07 · PDBe 7F07 · UniProt P06730
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