Research workbench
AlphaFold monomer V2.0 prediction for protein ndh-dependent cyclic electron flow 5 (Q9C503)
Analyse AlphaFold monomer V2.0 prediction for protein ndh-dependent cyclic electron… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9C503
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- Protein ndh-dependent cyclic electron flow 5
- UniProt
- Q9C503
- Pockets
- 6 · best druggability 0.55
Structure
1 distinct chain · 3% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein ndh-dependent cyclic electron flow 5 | protein | 354 | 3% helix, 49% strand | Q9C503 |
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 | 122 | 0.55 | 0.83 | 24 | empty |
| 2 | 169 | 0.51 | 0.78 | 26 | empty |
| 3 | 62 | 0.44 | 0.82 | 17 | empty |
| 4 | 196 | 0.43 | 0.73 | 27 | empty |
| 5 | 123 | 0.38 | 0.74 | 22 | 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 Q9C503
- Elsewhere: UniProt Q9C503 · AlphaFold DB Q9C503
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