Research workbench
AlphaFold monomer V2.0 prediction for 2-(HYDROXYMETHYL)GLUTARATE dehydrogenase (Q0QLF5)
Analyse AlphaFold monomer V2.0 prediction for 2-(HYDROXYMETHYL)GLUTARATE dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0QLF5
- Type
- protein
- Length
- 301 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- UniProt
- Q0QLF5
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 301 | — | Q0QLF5 |
Compared structures
- 3CKY · Structural and Kinetic Properties of a beta-hydroxyacid dehydrogenase involved in… · an experimental structure of the same protein · chain A against C, TM-score 0.96
- 3CKY · Structural and kinetic properties of a beta-hydroxyacid dehydrogenase involved in… · an experimental structure of the same protein · chain A against C, TM-score 0.96
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 Q0QLF5
- Elsewhere: UniProt Q0QLF5 · AlphaFold DB Q0QLF5
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