Research workbench
AlphaFold monomer V2.0 prediction for trans-aconitate 2-methyltransferase (B5ZUL2)
Analyse AlphaFold monomer V2.0 prediction for trans-aconitate 2-methyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5ZUL2
- Type
- protein
- Length
- 256 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- Trans-aconitate 2-methyltransferase
- UniProt
- B5ZUL2
- Pockets
- 1 · best druggability 0.74
Structure
1 distinct chain · 45% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trans-aconitate 2-methyltransferase | protein | 256 | 45% helix, 24% strand | B5ZUL2 |
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 | 416 | 0.74 | 0.84 | 62 | 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 B5ZUL2
- Elsewhere: UniProt B5ZUL2 · AlphaFold DB B5ZUL2
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