Research workbench
Crystal structure of JNK2
Analyse Crystal structure of JNK2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E7O
- Type
- protein
- Length
- 668 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 9
- EC
- 2.7.11.24
- UniProt
- P45984
- Ligands
- 35F
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 9 (EC 2.7.11.24) | protein | 342 | 38% helix, 16% strand | P45984 |
| B | Mitogen-activated protein kinase 9 (EC 2.7.11.24) | protein | 326 | 41% helix, 16% strand | P45984 |
Ligands and binding sites
- 35F · N-{3-[5-(1H-1,2,4-triazol-3-yl)-1H-indazol-3-yl]phenyl}furan-2-carboxamide · ligand · 2 copies · chains A, B
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 | 1117 | 0.74 | 0.77 | 86 | 35F |
| 2 | 386 | 0.63 | 0.78 | 40 | 35F |
| 3 | 138 | 0.45 | 0.77 | 17 | empty |
| 4 | 116 | 0.41 | 0.76 | 20 | empty |
| 5 | 72 | 0.31 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 364 Ų buried · 1 hydrogen bond · 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 P45984
- Elsewhere: RCSB PDB 3E7O · PDBe 3E7O · UniProt P45984
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