Research workbench
AlphaFold monomer V2.0 prediction for cysteine S-methyltransferase nlee (Q7DBA6)
Analyse AlphaFold monomer V2.0 prediction for cysteine S-methyltransferase nlee (Q7DBA6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7DBA6
- Type
- protein
- Length
- 224 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xCDcd2ae6FFfEe65c58bCB4fbDb0EC2F69303385C
- Molecule
- Cysteine S-methyltransferase nlee
- UniProt
- Q7DBA6
- Pockets
- 2 · best druggability 0.54
Structure
1 distinct chain · 49% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine S-methyltransferase nlee | protein | 224 | 49% helix, 12% strand | Q7DBA6 |
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 | 285 | 0.54 | 0.75 | 28 | empty |
| 2 | 71 | 0.33 | 0.75 | 21 | empty |
Compared structures
- 4R29 · Crystal structure of bacterial cysteine methyltransferase effector NleE · an experimental structure of the same protein · chain A against C, TM-score 0.89
- 4R29 · Crystal structure of bacterial cysteine methyltransferase effector nlee · an experimental structure of the same protein · chain A against C, TM-score 0.89
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 Q7DBA6
- Elsewhere: UniProt Q7DBA6 · AlphaFold DB Q7DBA6
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