Research workbench
AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase STE11 (P23561)
Analyse AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase STE11… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P23561
- Type
- protein
- Length
- 717 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7322182A904Ab8270621E3B35dc80C787052A76f
- Molecule
- SERINE/THREONINE-protein kinase STE11
- UniProt
- P23561
- Pockets
- 8 · best druggability 0.72
Structure
1 distinct chain · 38% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase STE11 | protein | 717 | 38% helix, 11% strand | P23561 |
Pockets
8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.72 | 0.97 | 17 | empty |
| 2 | 649 | 0.69 | 0.77 | 51 | empty |
| 3 | 228 | 0.61 | 0.81 | 34 | empty |
| 4 | 359 | 0.59 | 0.76 | 37 | empty |
| 5 | 209 | 0.56 | 0.79 | 23 | empty |
Compared structures
- 1X9X · Solution structure of dimeric SAM domain from mapkkk STE11 · an experimental structure of the same protein · chain A against A, TM-score 0.08
- 1X9X · Solution Structure of Dimeric SAM Domain from MAPKKK Ste11 · an experimental structure of the same protein · chain A against A, TM-score 0.08
- 1OW5 · NMR structure of the Saccharomyces cerevisiae SAM (Sterile Alpha Motif) domain · an experimental structure of the same protein · chain A against A, TM-score 0.08
- 1OW5 · NMR structure of the saccharomyces cerevisiae SAM (sterile alpha motif) domain · an experimental structure of the same protein · chain A against A, TM-score 0.08
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 P23561
- Elsewhere: UniProt P23561 · AlphaFold DB P23561
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