Research workbench
AlphaFold monomer V2.0 prediction for femo cofactor biosynthesis protein nifb (P46044)
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
- P46044
- Type
- protein
- Length
- 510 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Femo cofactor biosynthesis protein nifb
- UniProt
- P46044
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Femo cofactor biosynthesis protein nifb | protein | 510 | 35% helix, 17% strand | P46044 |
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 | 526 | 0.76 | 0.84 | 74 | empty |
| 2 | 247 | 0.60 | 0.80 | 35 | empty |
| 3 | 156 | 0.50 | 0.78 | 25 | empty |
| 4 | 179 | 0.48 | 0.76 | 25 | 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 P46044
- Elsewhere: UniProt P46044 · AlphaFold DB P46044
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