Research workbench
Crystal structure of MAP kinase P38 complexed to the docking site on its activator MKK3B
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
- 1LEZ
- 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; MAP kinase kinase 3B
- EC
- 2.7.1.-
- UniProt
- P47811
- Pockets
- 4 · best druggability 0.66
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 2.7.1.-) | protein | 343 | 41% helix, 15% strand | P47811 |
| B | MAP kinase kinase 3B | protein | 8 | 0% helix, 0% strand | — |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.66 | 0.81 | 42 | empty |
| 2 | 176 | 0.51 | 0.77 | 18 | empty |
| 3 | 243 | 0.50 | 0.75 | 39 | empty |
| 4 | 56 | 0.28 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 499 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1LEZ · Crystal structure of MAP kinase P38 complexed to the docking site on its activator MKK3B · 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
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
- Elsewhere: RCSB PDB 1LEZ · PDBe 1LEZ · UniProt P47811
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