Research workbench
AlphaFold monomer V2.0 prediction for dual specificity mitogen- activated protein kinase kinase 1 (P29678)
Analyse AlphaFold monomer V2.0 prediction for dual specificity mitogen- activated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P29678
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- Dual specificity mitogen-activated protein kinase kinase 1
- UniProt
- P29678
- Pockets
- 5 · best druggability 0.77
Structure
1 distinct chain · 43% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity mitogen-activated protein kinase kinase 1 | protein | 393 | 43% helix, 12% strand | P29678 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1178 | 0.77 | 0.79 | 118 | empty |
| 2 | 405 | 0.69 | 0.81 | 48 | empty |
| 3 | 83 | 0.49 | 0.83 | 22 | empty |
| 4 | 124 | 0.45 | 0.77 | 17 | empty |
| 5 | 114 | 0.39 | 0.75 | 21 | empty |
Compared structures
- 2Y4I · KSR2-MEK1 heterodimer · an experimental structure of the same protein · chain A against C, TM-score 0.78
- 2Y4I · KSR2-MEK1 heterodimer · an experimental structure of the same protein · chain A against C, TM-score 0.78
- 7JUY · Crystal Structure of KSR1:MEK1 in complex with AMP-PNP, and allosteric MEK inhibitor… · an experimental structure of the same protein · chain A against C, TM-score 0.78
- 7JUY · Crystal structure of KSR1:MEK1 in complex with AMP-pnp, and allosteric MEK inhibitor… · an experimental structure of the same protein · chain A against C, TM-score 0.78
- 7JUW · Crystal structure of KSR1:MEK1 in complex with AMP-pnp · an experimental structure of the same protein · chain A against C, TM-score 0.77
- 7JUW · Crystal Structure of KSR1:MEK1 in complex with AMP-PNP · an experimental structure of the same protein · chain A against C, TM-score 0.77
- 5KKR · KSR2:MEK1 Complex Bound to the Small Molecule APS-2-79 · an experimental structure of the same protein · chain A against C, TM-score 0.77
- 5KKR · KSR2:MEK1 complex bound to the small molecule aps-2-79 · an experimental structure of the same protein · chain A against C, TM-score 0.77
- 7JUZ · Crystal structure of KSR1:MEK1 in complex with AMP-pnp, and allosteric MEK inhibitor… · an experimental structure of the same protein · chain A against C, TM-score 0.77
- 7JUZ · Crystal Structure of KSR1:MEK1 in complex with AMP-PNP, and allosteric MEK inhibitor… · an experimental structure of the same protein · chain A against C, TM-score 0.77
- 7JV0 · Crystal structure of KSR1:MEK1 in complex with AMP-pnp, and allosteric MEK inhibitor… · an experimental structure of the same protein · chain A against C, TM-score 0.77
- 7JV0 · Crystal Structure of KSR1:MEK1 in complex with AMP-PNP, and allosteric MEK inhibitor… · an experimental structure of the same protein · chain A against C, TM-score 0.77
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 P29678
- Elsewhere: UniProt P29678 · AlphaFold DB P29678
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