Research workbench
AlphaFold monomer V2.0 prediction for femo cofactor biosynthesis protein nifb (P24427)
Analyse AlphaFold monomer V2.0 prediction for femo cofactor biosynthesis protein nifb… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P24427
- Type
- protein
- Length
- 490 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF2f87f077Bf4C1656e09B41684f4F18Dd78B5BC2
- Molecule
- Femo cofactor biosynthesis protein nifb
- UniProt
- P24427
- Pockets
- 6 · best druggability 0.76
Structure
1 distinct chain · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Femo cofactor biosynthesis protein nifb | protein | 490 | 35% helix, 19% strand | P24427 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1000 | 0.76 | 0.79 | 77 | empty |
| 2 | 109 | 0.50 | 0.81 | 18 | empty |
| 3 | 77 | 0.48 | 0.83 | 19 | empty |
| 4 | 146 | 0.44 | 0.76 | 22 | empty |
| 5 | 83 | 0.35 | 0.75 | 15 | 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 P24427
- Elsewhere: UniProt P24427 · AlphaFold DB P24427
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