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Crystal structure of human JNK3 complexed with N-(3-cyano-4,5,6,7- tetrahydro-1-benzothien-2-yl)-2-fluorobenzamide
Analyse Crystal structure of human JNK3 complexed with N-(3-cyano-4,5,6,7… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O2U
- Type
- protein
- Length
- 319 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 10
- EC
- 2.7.11.24
- UniProt
- P53779
- Ligands
- 738
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 10 (EC 2.7.11.24) | protein | 319 | 42% helix, 17% strand | P53779 |
Ligands and binding sites
- 738 · N-(3-cyano-4,5,6,7-tetrahydro-1-benzothien-2-yl)-2-fluorobenzamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 393 | 0.70 | 0.82 | 40 | 738 |
| 2 | 58 | 0.32 | 0.76 | 16 | empty |
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 P53779
- Elsewhere: RCSB PDB 2O2U · PDBe 2O2U · UniProt P53779
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