MolNFT v1 · #275654 · protein
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (B5EFG0)
B5EFG0: “AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (B5EFG0)”. 3 pockets (best druggability 0.45). MolNFT v1 #275654 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- B5EFG0
- Type
- protein
- Length
- 389 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4BC59faea63ACA4315D24e40823D4B8bF16F1540
- Molecule
- NADH-quinone oxidoreductase subunit D
- UniProt
- B5EFG0
- Pockets
- 3 · best druggability 0.45
Structure
1 distinct chain · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit D | protein | 389 | 52% helix, 13% strand | B5EFG0 |
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 | 53 | 0.45 | 0.84 | 16 | empty |
| 2 | 56 | 0.37 | 0.79 | 17 | empty |
| 3 | 64 | 0.31 | 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 B5EFG0
- Elsewhere: UniProt B5EFG0 · AlphaFold DB B5EFG0
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