Research workbench
AlphaFold monomer V2.0 prediction for NAD-dependent malic enzyme (B5FHJ6)
Analyse AlphaFold monomer V2.0 prediction for NAD-dependent malic enzyme (B5FHJ6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5FHJ6
- Type
- protein
- Length
- 565 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9bF5F84C75690a56a78965Df98E262fC9c087f0C
- Molecule
- NAD-dependent malic enzyme
- UniProt
- B5FHJ6
- Pockets
- 7 · best druggability 0.77
Structure
1 distinct chain · 49% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent malic enzyme | protein | 565 | 49% helix, 11% strand | B5FHJ6 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 642 | 0.77 | 0.82 | 82 | empty |
| 2 | 81 | 0.74 | 0.97 | 27 | empty |
| 3 | 464 | 0.66 | 0.78 | 47 | empty |
| 4 | 104 | 0.53 | 0.82 | 24 | empty |
| 5 | 128 | 0.45 | 0.77 | 20 | 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 B5FHJ6
- Elsewhere: UniProt B5FHJ6 · AlphaFold DB B5FHJ6
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