Research workbench
AlphaFold monomer V2.0 prediction for femo cofactor biosynthesis protein nifb (P11067)
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
- P11067
- Type
- protein
- Length
- 502 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Femo cofactor biosynthesis protein nifb
- UniProt
- P11067
- Pockets
- 4 · best druggability 0.77
Structure
1 distinct chain · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Femo cofactor biosynthesis protein nifb | protein | 502 | 39% helix, 16% strand | P11067 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 796 | 0.77 | 0.81 | 65 | empty |
| 2 | 395 | 0.65 | 0.79 | 41 | empty |
| 3 | 91 | 0.46 | 0.81 | 19 | empty |
| 4 | 82 | 0.40 | 0.78 | 18 | 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 P11067
- Elsewhere: UniProt P11067 · AlphaFold DB P11067
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