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The structure of P38ALPHA
Analyse The structure of P38ALPHA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R39
- Type
- protein
- Length
- 345 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
- Q16539
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 14 (EC 2.7.1.37) | protein | 345 | 41% helix, 16% strand | Q16539 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 503 | 0.66 | 0.78 | 52 | empty |
| 2 | 145 | 0.48 | 0.77 | 21 | empty |
| 3 | 87 | 0.38 | 0.76 | 17 | empty |
| 4 | 52 | 0.34 | 0.78 | 12 | empty |
| 5 | 53 | 0.33 | 0.77 | 17 | empty |
Compared structures
- 1R39 · The structure of P38ALPHA · 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 1R39 · PDBe 1R39 · UniProt Q16539
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