Research workbench
AlphaFold monomer V2.0 prediction for femo cofactor biosynthesis protein nifb (D5VRM1)
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
- D5VRM1
- Type
- protein
- Length
- 302 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e17C80A3064A18cE97C3a90e5C69D9a222F548e
- Molecule
- Femo cofactor biosynthesis protein nifb
- UniProt
- D5VRM1
- Pockets
- 3 · best druggability 0.87
Structure
1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Femo cofactor biosynthesis protein nifb | protein | 302 | 39% helix, 20% strand | D5VRM1 |
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 | 427 | 0.87 | 0.95 | 57 | empty |
| 2 | 83 | 0.45 | 0.81 | 18 | empty |
| 3 | 82 | 0.39 | 0.77 | 21 | 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 D5VRM1
- Elsewhere: UniProt D5VRM1 · AlphaFold DB D5VRM1
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