Research workbench
AlphaFold monomer V2.0 prediction for F420-non-reducing hydrogenase vhc subunit a (Q00404)
Analyse AlphaFold monomer V2.0 prediction for F420-non-reducing hydrogenase vhc subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q00404
- Type
- protein
- Length
- 474 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- F420-non-reducing hydrogenase vhc subunit a
- UniProt
- Q00404
- Pockets
- 4 · best druggability 0.45
Structure
1 distinct chain · 45% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F420-non-reducing hydrogenase vhc subunit a | protein | 474 | 45% helix, 21% strand | Q00404 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 185 | 0.45 | 0.75 | 33 | empty |
| 2 | 135 | 0.44 | 0.76 | 19 | empty |
| 3 | 110 | 0.41 | 0.76 | 23 | empty |
| 4 | 92 | 0.38 | 0.76 | 20 | 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 Q00404
- Elsewhere: UniProt Q00404 · AlphaFold DB Q00404
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