Research workbench
AlphaFold monomer V2.0 prediction for femo cofactor biosynthesis protein nifb (P20627)
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
- P20627
- Type
- protein
- Length
- 475 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7782F4817b37743d738e9aF842bf74bd50f2015E
- Molecule
- Femo cofactor biosynthesis protein nifb
- UniProt
- P20627
- Pockets
- 6 · best druggability 0.74
Structure
1 distinct chain · 37% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Femo cofactor biosynthesis protein nifb | protein | 475 | 37% helix, 20% strand | P20627 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.74 | 0.99 | 24 | empty |
| 2 | 747 | 0.68 | 0.75 | 48 | empty |
| 3 | 274 | 0.60 | 0.79 | 35 | empty |
| 4 | 109 | 0.49 | 0.81 | 17 | empty |
| 5 | 77 | 0.41 | 0.79 | 16 | 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 P20627
- Elsewhere: UniProt P20627 · AlphaFold DB P20627
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