Research workbench
AlphaFold monomer V2.0 prediction for citrate synthase-lysine N-methyltransferase cskmt, mitochondrial (A8MUP2)
Analyse AlphaFold monomer V2.0 prediction for citrate synthase-lysine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A8MUP2
- Type
- protein
- Length
- 240 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- Citrate synthase-lysine N-methyltransferase cskmt, mitochondrial
- UniProt
- A8MUP2
- Pockets
- 2 · best druggability 0.72
Structure
1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Citrate synthase-lysine N-methyltransferase cskmt, mitochondrial | protein | 240 | 30% helix, 26% strand | A8MUP2 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 389 | 0.72 | 0.83 | 49 | empty |
| 2 | 60 | 0.28 | 0.73 | 20 | 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 A8MUP2
- Elsewhere: UniProt A8MUP2 · AlphaFold DB A8MUP2
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