Research workbench
AlphaFold monomer V2.0 prediction for cytosolic fe-S cluster assembly factor NUBP1 homolog (Q29MT7)
Analyse AlphaFold monomer V2.0 prediction for cytosolic fe-S cluster assembly factor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q29MT7
- Type
- protein
- Length
- 311 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x507b0cF5c2F663afF8A05761eBf4e0Bf457a72Fb
- Molecule
- Cytosolic fe-S cluster assembly factor NUBP1 homolog
- UniProt
- Q29MT7
- Pockets
- 3 · best druggability 0.48
Structure
1 distinct chain · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytosolic fe-S cluster assembly factor NUBP1 homolog | protein | 311 | 34% helix, 20% strand | Q29MT7 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 202 | 0.48 | 0.75 | 35 | empty |
| 2 | 71 | 0.46 | 0.82 | 17 | empty |
| 3 | 51 | 0.31 | 0.77 | 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 Q29MT7
- Elsewhere: UniProt Q29MT7 · AlphaFold DB Q29MT7
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