Research workbench
AlphaFold monomer V2.0 prediction for isethionate sulfite-lyase (E5Y378)
Analyse AlphaFold monomer V2.0 prediction for isethionate sulfite-lyase (E5Y378) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- E5Y378
- Type
- protein
- Length
- 830 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- UniProt
- E5Y378
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 830 | — | E5Y378 |
Compared structures
- 7KQ4 · Structure of isethionate sulfite-lyase from Bilophila wadsworthia with glycerol bound · an experimental structure of the same protein · chain A against B, TM-score 0.99
- 7KQ3 · Structure of isethionate sulfite-lyase from Bilophila wadsworthia with substrate… · an experimental structure of the same protein · chain A against D, TM-score 0.99
- 7KQ4 · Structure of isethionate sulfite-lyase from bilophila wadsworthia with glycerol bound · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 7KQ3 · Structure of isethionate sulfite-lyase from bilophila wadsworthia with substrate… · an experimental structure of the same protein · chain A against A, 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 E5Y378
- Elsewhere: UniProt E5Y378 · AlphaFold DB E5Y378
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