MolNFT v1 · #87421 · protein
Mammalian translation elongation factor EEF1A2
4C0S · Elongation factor 1-alpha 2: “Mammalian translation elongation factor EEF1A2”. X-ray diffraction, 2 ligands (GDP, MG), 13 pockets (best druggability 0.74). MolNFT v1 #87421 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4C0S
- Type
- protein
- Length
- 893 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor 1-alpha 2
- UniProt
- Q71V39
- Ligands
- GDP, MG
- Pockets
- 13 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor 1-alpha 2 | protein | 451 | 22% helix, 31% strand | Q71V39 |
| B | Elongation factor 1-alpha 2 | protein | 442 | 21% helix, 34% strand | Q71V39 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 834 | 0.74 | 0.78 | 87 | empty |
| 2 | 466 | 0.68 | 0.79 | 43 | empty |
| 3 | 153 | 0.61 | 0.84 | 26 | empty |
| 4 | 98 | 0.59 | 0.87 | 22 | empty |
| 5 | 164 | 0.58 | 0.82 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 2548 Ų buried · 34 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
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 Q71V39
- Elsewhere: RCSB PDB 4C0S · PDBe 4C0S · UniProt Q71V39
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