Research workbench
Crystal structure of the P38A-mapkap kinase 2 heterodimer
Analyse Crystal structure of the P38A-mapkap kinase 2 heterodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OKR
- Type
- protein
- Length
- 726 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 14; MAP kinase-activated protein kinase 2
- EC
- 2.7.11.24, 2.7.11.1
- UniProt
- Q16539, P49137
- Pockets
- 10 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 14 (EC 2.7.11.24) | protein | 339 | 40% helix, 16% strand | Q16539 |
| C, F | MAP kinase-activated protein kinase 2 (EC 2.7.11.1) | protein | 24 | 38% helix, 0% strand | P49137 |
| D | Mitogen-activated protein kinase 14 (EC 2.7.11.24) | protein | 339 | 39% helix, 15% strand | Q16539 |
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.64 | 0.80 | 45 | empty |
| 2 | 312 | 0.62 | 0.79 | 36 | empty |
| 3 | 131 | 0.42 | 0.75 | 20 | empty |
| 4 | 98 | 0.39 | 0.76 | 18 | empty |
| 5 | 119 | 0.39 | 0.74 | 25 | empty |
Interfaces
4 interfaces between chains.
- D–F · 924 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 895 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 574 Ų buried · 6 hydrogen bonds · protein-protein
- A–F · 114 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2OKR · Crystal Structure of the P38a-MAPKAP kinase 2 Heterodimer · 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
- Every structure of UniProt P49137
- Elsewhere: RCSB PDB 2OKR · PDBe 2OKR · UniProt Q16539 · UniProt P49137
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