Research workbench
Structure of P38ALPHA complex
Analyse Structure of P38ALPHA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OZA
- Type
- protein
- Length
- 672 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MAP kinase-activated protein kinase 2; Mitogen-activated protein kinase 14
- EC
- 2.7.11.1, 2.7.11.24
- UniProt
- P49137, P47811
- Pockets
- 11 · best druggability 0.89
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MAP kinase-activated protein kinase 2 (EC 2.7.11.1) | protein | 332 | 38% helix, 19% strand | P49137 |
| B | Mitogen-activated protein kinase 14 (EC 2.7.11.24) | protein | 340 | 37% helix, 12% strand | P47811 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1071 | 0.89 | 0.91 | 137 | empty |
| 2 | 156 | 0.59 | 0.83 | 21 | empty |
| 3 | 129 | 0.54 | 0.82 | 22 | empty |
| 4 | 130 | 0.54 | 0.82 | 17 | empty |
| 5 | 206 | 0.47 | 0.75 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 3350 Ų buried · 55 hydrogen bonds · protein-protein
Compared structures
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 P49137
- Every structure of UniProt P47811
- Elsewhere: RCSB PDB 2OZA · PDBe 2OZA · UniProt P49137 · UniProt P47811
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