Research workbench
AlphaFold monomer V2.0 prediction for 4-hydroxy- tetrahydrodipicolinate reductase (Q3MFY8)
Analyse AlphaFold monomer V2.0 prediction for 4-hydroxy- tetrahydrodipicolinate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q3MFY8
- Type
- protein
- Length
- 278 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x54E712e282c590D9A20961451A63f1380e0a3dD4
- UniProt
- Q3MFY8
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 278 | — | Q3MFY8 |
Compared structures
- 5KT0 · Dihydrodipicolinate reductase from the industrial and evolutionarily important… · an experimental structure of the same protein · chain A against A, TM-score 0.89
- 5KT0 · Dihydrodipicolinate reductase from the industrial and evolutionarily important… · an experimental structure of the same protein · chain A against A, TM-score 0.89
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 Q3MFY8
- Elsewhere: UniProt Q3MFY8 · AlphaFold DB Q3MFY8
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