Research workbench
Crystal structure of P38 alpha MAP kinase in complex with a novel isoform selective drug candidate
Analyse Crystal structure of P38 alpha MAP kinase in complex with a novel isoform… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R3C
- 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
- 2.7.11.24
- UniProt
- Q16539
- Ligands
- 3GF, GG5, CL
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 14 (EC 2.7.11.24) | protein | 336 | 43% helix, 16% strand | Q16539 |
Ligands and binding sites
- 3GF · 6-(4-methylpiperazin-1-yl)-3-(naphthalen-2-yl)-4-(pyridin-4-yl)pyridazine · ligand · 2 copies · chains A
- GG5 · 4-[3-(4-fluorophenyl)-1H-pyrazol-4-yl]pyridine · ligand · chains A
- CL · Chloride ion · ion · 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 | 489 | 0.68 | 0.79 | 48 | 3GF, CL |
| 2 | 110 | 0.68 | 0.90 | 20 | GG5 |
| 3 | 121 | 0.39 | 0.74 | 18 | empty |
| 4 | 90 | 0.38 | 0.76 | 19 | empty |
| 5 | 50 | 0.26 | 0.73 | 16 | empty |
Modifications
Observed in the structure: 1 modified (artifact).
Compared structures
- 4R3C · Crystal structure of p38 alpha MAP kinase in complex with a novel isoform selective drug… · the same entry in another collection · chain A against A, TM-score 1.00
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
- Elsewhere: RCSB PDB 4R3C · PDBe 4R3C · UniProt Q16539
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