Research workbench
Mutated MAP kinase P38 (mus musculus) in complex with inhbitor pg- 895449
Analyse Mutated MAP kinase P38 (mus musculus) in complex with inhbitor pg- 895449 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GHM
- Type
- protein
- Length
- 336 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 14
- EC
- 2.7.1.37
- UniProt
- P47811
- Ligands
- LIC
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 14 (EC 2.7.1.37) | protein | 336 | 38% helix, 15% strand | P47811 |
Ligands and binding sites
- LIC · 3-(2-chlorobenzyl)-1-(2-{[(1S)-2-hydroxy-1,2-dimethylpropyl]amino}pyrimidin-4-yl)-1-(4-methoxyphenyl)urea · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 424 | 0.69 | 0.80 | 44 | LIC |
| 2 | 104 | 0.67 | 0.90 | 21 | empty |
| 3 | 113 | 0.41 | 0.76 | 18 | empty |
| 4 | 73 | 0.34 | 0.76 | 18 | empty |
| 5 | 51 | 0.29 | 0.75 | 13 | empty |
Compared structures
- 2GHM · Mutated MAP kinase P38 (Mus Musculus) in complex with Inhbitor PG-895449 · 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 0.99
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 2GHM · PDBe 2GHM · UniProt P47811
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