Research workbench
Nucleotide exchange mechanisms in the EEF1A-EEF1BA complex
Analyse Nucleotide exchange mechanisms in the EEF1A-EEF1BA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IJF
- Type
- protein
- Length
- 530 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
- GDP, MG
- Pockets
- 6 · best druggability 0.80
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 | 440 | 22% helix, 34% strand | P02994 |
| B | Elongation factor 1-beta | protein | 90 | 19% helix, 49% strand | P32471 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1001 | 0.80 | 0.82 | 102 | empty |
| 2 | 175 | 0.61 | 0.83 | 34 | MG, GDP |
| 3 | 119 | 0.40 | 0.75 | 19 | empty |
| 4 | 88 | 0.40 | 0.77 | 15 | empty |
| 5 | 81 | 0.37 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1836 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 1IJF · Nucleotide exchange mechanisms in the eEF1A-eEF1Ba complex · the same entry in another collection · chain A against A, 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 0.98
- 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 0.80
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 1IJF · PDBe 1IJF · UniProt P02994 · UniProt P32471
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