Research workbench
AlphaFold monomer V2.0 prediction for NFU1 iron-sulfur cluster scaffold homolog, mitochondrial (B4NE93)
Analyse AlphaFold monomer V2.0 prediction for NFU1 iron-sulfur cluster scaffold… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B4NE93
- Type
- protein
- Length
- 289 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD658EdA82c91e0f47BE623f902f6e81aA4f0b51e
- Molecule
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- UniProt
- B4NE93
- Pockets
- 3 · best druggability 0.42
Structure
1 distinct chain · 33% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NFU1 iron-sulfur cluster scaffold homolog, mitochondrial | protein | 289 | 33% helix, 15% strand | B4NE93 |
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 | 120 | 0.42 | 0.77 | 19 | empty |
| 2 | 116 | 0.40 | 0.75 | 17 | empty |
| 3 | 64 | 0.32 | 0.76 | 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 B4NE93
- Elsewhere: UniProt B4NE93 · AlphaFold DB B4NE93
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