MolNFT v1 · #118155 · protein
Structure of dead kinase MAPK14 with bound the kim domain of MKK6
5ETF · Mitogen-activated protein kinase 14: “Structure of dead kinase MAPK14 with bound the kim domain of MKK6”. X-ray diffraction, 4 pockets (best druggability 0.67). MolNFT v1 #118155 on GenesisL1: 3D structure, binding sites and pockets…
- 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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