Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit H, chloroplastic (B5LMS0)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit H… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5LMS0
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- NAD(P)H-quinone oxidoreductase subunit H, chloroplastic
- UniProt
- B5LMS0
- Pockets
- 3 · best druggability 0.60
Structure
1 distinct chain · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit H, chloroplastic | protein | 393 | 48% helix, 12% strand | B5LMS0 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.60 | 0.80 | 39 | empty |
| 2 | 63 | 0.49 | 0.84 | 18 | empty |
| 3 | 74 | 0.32 | 0.75 | 12 | 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 B5LMS0
- Elsewhere: UniProt B5LMS0 · AlphaFold DB B5LMS0
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