Research workbench
AlphaFold monomer V2.0 prediction for 2-isopropylmalate synthase (Q326G1)
Analyse AlphaFold monomer V2.0 prediction for 2-isopropylmalate synthase (Q326G1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q326G1
- Type
- protein
- Length
- 523 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- 2-isopropylmalate synthase
- UniProt
- Q326G1
- Pockets
- 4 · best druggability 0.53
Structure
1 distinct chain · 46% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2-isopropylmalate synthase | protein | 523 | 46% helix, 21% strand | Q326G1 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.53 | 0.79 | 28 | empty |
| 2 | 148 | 0.43 | 0.75 | 20 | empty |
| 3 | 99 | 0.41 | 0.77 | 18 | empty |
| 4 | 65 | 0.38 | 0.79 | 15 | empty |
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 Q326G1
- Elsewhere: UniProt Q326G1 · AlphaFold DB Q326G1
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