Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (B2JDM5)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2JDM5
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7beC3Ef9c210E66D52B594848B0A7dB52F1cD5c4
- Molecule
- NADH-quinone oxidoreductase subunit D
- UniProt
- B2JDM5
- Pockets
- 3 · best druggability 0.50
Structure
1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit D | protein | 417 | 52% helix, 12% strand | B2JDM5 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.50 | 0.84 | 20 | empty |
| 2 | 72 | 0.30 | 0.73 | 14 | empty |
| 3 | 77 | 0.29 | 0.72 | 14 | 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 B2JDM5
- Elsewhere: UniProt B2JDM5 · AlphaFold DB B2JDM5
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