Research workbench
AlphaFold monomer V2.0 prediction for 3-dehydroquinate dehydratase (Q5SIL5)
Analyse AlphaFold monomer V2.0 prediction for 3-dehydroquinate dehydratase (Q5SIL5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5SIL5
- Type
- protein
- Length
- 149 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- 3-dehydroquinate dehydratase
- UniProt
- Q5SIL5
- Pockets
- 1 · best druggability 0.63
Structure
1 distinct chain · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-dehydroquinate dehydratase | protein | 149 | 46% helix, 16% strand | Q5SIL5 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 89 | 0.63 | 0.90 | 18 | empty |
Compared structures
- 2UYG · Crystallogaphic structure of the typeII 3-Dehydroquinase from Thermus Thermophilus · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 2UYG · Crystallogaphic structure of the typeii 3-dehydroquinase from thermus thermophilus · an experimental structure of the same protein · chain A against A, TM-score 0.94
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 Q5SIL5
- Elsewhere: UniProt Q5SIL5 · AlphaFold DB Q5SIL5
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