Research workbench
AlphaFold monomer V2.0 prediction for short-chain DEHYDROGENASE/REDUCTASE malc (L0E4F8)
Analyse AlphaFold monomer V2.0 prediction for short-chain DEHYDROGENASE/REDUCTASE malc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- L0E4F8
- Type
- protein
- Length
- 264 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- UniProt
- L0E4F8
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 264 | — | L0E4F8 |
Compared structures
- 6NKH · Structure of MalC Reductase/Diels-Alderase from Malbranchea aurantiaca · an experimental structure of the same protein · chain A against A, TM-score 0.96
- 6NKH · Structure of malc REDUCTASE/DIELS-alderase from malbranchea aurantiaca · an experimental structure of the same protein · chain A against A, 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 L0E4F8
- Elsewhere: UniProt L0E4F8 · AlphaFold DB L0E4F8
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