Research workbench
AlphaFold monomer V2.0 prediction for elongation factor tu, chloroplastic (Q1KVS9)
Analyse AlphaFold monomer V2.0 prediction for elongation factor tu, chloroplastic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1KVS9
- Type
- protein
- Length
- 419 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- Elongation factor tu, chloroplastic
- UniProt
- Q1KVS9
- Pockets
- 5 · best druggability 0.60
Structure
1 distinct chain · 23% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor tu, chloroplastic | protein | 419 | 23% helix, 36% strand | Q1KVS9 |
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 | 300 | 0.60 | 0.78 | 33 | empty |
| 2 | 354 | 0.60 | 0.77 | 38 | empty |
| 3 | 72 | 0.45 | 0.82 | 24 | empty |
| 4 | 114 | 0.42 | 0.76 | 18 | empty |
| 5 | 60 | 0.31 | 0.75 | 16 | 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 Q1KVS9
- Elsewhere: UniProt Q1KVS9 · AlphaFold DB Q1KVS9
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