Research workbench
Crystal structure analysis of the yeast elongation factor complex EEF1A:EEF1BA
Analyse Crystal structure analysis of the yeast elongation factor complex EEF1A:EEF1BA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O8W
- Type
- protein
- Length
- 542 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor 1-alpha; Elongation factor 1-beta
- UniProt
- P02994, P32471
- Ligands
- GLN
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor 1-alpha | protein | 449 | 23% helix, 35% strand | P02994 |
| B | Elongation factor 1-beta | protein | 93 | 18% helix, 47% strand | P32471 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1186 | 0.78 | 0.80 | 105 | empty |
| 2 | 272 | 0.63 | 0.81 | 56 | empty |
| 3 | 88 | 0.43 | 0.80 | 15 | empty |
| 4 | 88 | 0.39 | 0.77 | 15 | empty |
| 5 | 103 | 0.37 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1858 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified, 1 covalent (engineered, methylation, covalent ligand).
Compared structures
- 5O8W · Crystal structure analysis of the yeast elongation factor complex EEF1A:EEF1BA · the same entry in another collection · chain B against B, TM-score 1.00
- P32471 · AlphaFold monomer V2.0 prediction for elongation factor 1-beta (P32471) · a predicted model of the same protein · chain B against A, TM-score 0.96
- P02994 · AlphaFold monomer V2.0 prediction for elongation factor 1-alpha (P02994) · a predicted model of the same protein · chain A against A, TM-score 0.79
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 P02994
- Every structure of UniProt P32471
- Elsewhere: RCSB PDB 5O8W · PDBe 5O8W · UniProt P02994 · UniProt P32471
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