Research workbench
AlphaFold monomer V2.0 prediction for nitrogenase iron-molybdenum cofactor biosynthesis protein nife (P95297)
Analyse AlphaFold monomer V2.0 prediction for nitrogenase iron-molybdenum cofactor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P95297
- Type
- protein
- Length
- 480 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Nitrogenase iron-molybdenum cofactor biosynthesis protein nife
- UniProt
- P95297
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitrogenase iron-molybdenum cofactor biosynthesis protein nife | protein | 480 | 47% helix, 15% strand | P95297 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 367 | 0.76 | 0.86 | 46 | empty |
| 2 | 107 | 0.37 | 0.74 | 19 | empty |
| 3 | 64 | 0.32 | 0.75 | 17 | empty |
| 4 | 55 | 0.29 | 0.75 | 17 | 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 P95297
- Elsewhere: UniProt P95297 · AlphaFold DB P95297
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