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AlphaFold monomer V2.0 prediction for F420-non-reducing hydrogenase iron-sulfur subunit a (P84625)
Analyse AlphaFold monomer V2.0 prediction for F420-non-reducing hydrogenase iron-sulfur… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P84625
- Type
- protein
- Length
- 486 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x85B6B478711D4a6F442F2c82D8D795D37aDC473d
- Molecule
- F420-non-reducing hydrogenase iron-sulfur subunit a
- UniProt
- P84625
- Pockets
- 2 · best druggability 0.45
Structure
1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F420-non-reducing hydrogenase iron-sulfur subunit a | protein | 486 | 44% helix, 21% strand | P84625 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.45 | 0.75 | 30 | empty |
| 2 | 97 | 0.34 | 0.73 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P84625
- Elsewhere: UniProt P84625 · AlphaFold DB P84625
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