Research workbench
Complex crystal structure of ascaris suum EIF4E-3 with M2,2,7G cap
Analyse Complex crystal structure of ascaris suum EIF4E-3 with M2,2,7G cap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M94
- Type
- protein
- Length
- 193 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Translation initiation factor 4E; Eukaryotic translation initiation factor 4E-binding…
- UniProt
- Q6PKX2, Q13541
- Ligands
- M7M, ACE
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Translation initiation factor 4E | protein | 180 | 29% helix, 31% strand | Q6PKX2 |
| C | Eukaryotic translation initiation factor 4E-binding protein 1 | protein | 13 | 54% helix, 0% strand | Q13541 |
Ligands and binding sites
- M7M · N,N,7-trimethylguanosine 5'-(trihydrogen diphosphate) · ligand · chains A
- ACE · Acetyl group · ligand · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.33 | 0.75 | 17 | M7M |
Interfaces
1 interface between chains.
- A–C · 715 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 3M94 · Complex crystal structure of Ascaris suum eIF4E-3 with m2,2,7G cap · the same entry in another collection · chain C against C, TM-score 1.00
- Q13541 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 4E-binding… · a predicted model of the same protein · chain C against A, TM-score 0.65
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 Q6PKX2
- Every structure of UniProt Q13541
- Elsewhere: RCSB PDB 3M94 · PDBe 3M94 · UniProt Q6PKX2 · UniProt Q13541
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