Research workbench
AlphaFold monomer V2.0 prediction for benzaldehyde dehydrogenase [NAD(+)] (P43503)
Analyse AlphaFold monomer V2.0 prediction for benzaldehyde dehydrogenase [NAD(+)]… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P43503
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x627DfEbfC08CCF86E151D6C3143e17Eada033427
- Molecule
- Benzaldehyde dehydrogenase [NAD(+)]
- UniProt
- P43503
- Pockets
- 3 · best druggability 0.61
Structure
1 distinct chain · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Benzaldehyde dehydrogenase [NAD(+)] | protein | 487 | 42% helix, 22% strand | P43503 |
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 | 301 | 0.61 | 0.78 | 36 | empty |
| 2 | 107 | 0.46 | 0.78 | 20 | empty |
| 3 | 72 | 0.40 | 0.79 | 17 | 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 P43503
- Elsewhere: UniProt P43503 · AlphaFold DB P43503
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