Research workbench
AlphaFold monomer V2.0 prediction for elongation factor tu, mitochondrial (Q54HB2)
Analyse AlphaFold monomer V2.0 prediction for elongation factor tu, mitochondrial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q54HB2
- Type
- protein
- Length
- 424 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- Elongation factor tu, mitochondrial
- UniProt
- Q54HB2
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 23% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor tu, mitochondrial | protein | 424 | 23% helix, 33% strand | Q54HB2 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 322 | 0.64 | 0.80 | 42 | empty |
| 2 | 299 | 0.58 | 0.77 | 35 | empty |
| 3 | 71 | 0.44 | 0.82 | 24 | empty |
| 4 | 115 | 0.41 | 0.76 | 25 | empty |
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 Q54HB2
- Elsewhere: UniProt Q54HB2 · AlphaFold DB Q54HB2
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