Research workbench
Structure of dead kinase MAPK14 with bound the kim domain of MKK6
Analyse Structure of dead kinase MAPK14 with bound the kim domain of MKK6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ETF
- Type
- protein
- Length
- 346 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 14; Dual specificity mitogen-activated protein kinase…
- EC
- 2.7.11.24, 2.7.12.2
- UniProt
- Q16539, P52564
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 14 (EC 2.7.11.24) | protein | 338 | 40% helix, 14% strand | Q16539 |
| B | Dual specificity mitogen-activated protein kinase kinase 6 (EC 2.7.12.2) | protein | 8 | 0% helix, 0% strand | P52564 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 438 | 0.67 | 0.79 | 50 | empty |
| 2 | 207 | 0.51 | 0.76 | 29 | empty |
| 3 | 156 | 0.45 | 0.75 | 32 | empty |
| 4 | 61 | 0.30 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 504 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5ETF · Structure of dead kinase MAPK14 with bound the KIM domain of MKK6 · the same entry in another collection · chain A against A, TM-score 1.00
- P52564 · AlphaFold monomer V2.0 prediction for dual specificity mitogen- activated protein kinase… · a predicted model of the same protein · chain B against A, TM-score 0.52
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 Q16539
- Every structure of UniProt P52564
- Elsewhere: RCSB PDB 5ETF · PDBe 5ETF · UniProt Q16539 · UniProt P52564
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