Research workbench
Crystal structure of MAP kinase P38 complexed to the docking site on its nuclear substrate MEF2A
Analyse Crystal structure of MAP kinase P38 complexed to the docking site on its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LEW
- Type
- protein
- Length
- 351 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 14; Myocyte-specific enhancer factor 2A
- EC
- 2.7.11.24
- UniProt
- P47811, Q02078
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 14 (EC 2.7.11.24) | protein | 341 | 41% helix, 16% strand | P47811 |
| B | Myocyte-specific enhancer factor 2A | protein | 10 | 0% helix, 0% strand | Q02078 |
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 | 383 | 0.65 | 0.79 | 44 | empty |
| 2 | 257 | 0.53 | 0.76 | 41 | empty |
| 3 | 64 | 0.49 | 0.85 | 15 | empty |
| 4 | 112 | 0.41 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 569 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1LEW · Crystal structure of MAP kinase P38 complexed to the docking site on its nuclear… · the same entry in another collection · chain A against A, TM-score 1.00
- P47811 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase 14 (P47811) · a predicted model of the same protein · chain A against A, TM-score 0.97
- Q02078 · AlphaFold monomer V2.0 prediction for myocyte-specific enhancer factor 2A (Q02078) · a predicted model of the same protein · chain B against A, TM-score 0.46
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 P47811
- Every structure of UniProt Q02078
- Elsewhere: RCSB PDB 1LEW · PDBe 1LEW · UniProt P47811 · UniProt Q02078
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