Research workbench
AlphaFold monomer V2.0 prediction for formate dehydrogenase (G0SGU4)
Analyse AlphaFold monomer V2.0 prediction for formate dehydrogenase (G0SGU4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- G0SGU4
- Type
- protein
- Length
- 370 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- UniProt
- G0SGU4
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 370 | — | G0SGU4 |
Compared structures
- 6T8Z · NAD+-dependent fungal formate dehydrogenase from Chaetomium thermophilum: A ternary… · an experimental structure of the same protein · chain A against CCC, TM-score 1.00
- 6T8Y · NAD+-dependent fungal formate dehydrogenase from Chaetomium thermophilum: A complex with… · an experimental structure of the same protein · chain A against CCC, TM-score 1.00
- 6T94 · NAD+-dependent fungal formate dehydrogenase from Chaetomium thermophilum: A complex of… · an experimental structure of the same protein · chain A against BBB, TM-score 0.99
- 6T92 · NAD+-dependent fungal formate dehydrogenase from Chaetomium thermophilum: A complex of… · an experimental structure of the same protein · chain A against CCC, TM-score 0.99
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 G0SGU4
- Elsewhere: UniProt G0SGU4 · AlphaFold DB G0SGU4
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