Research workbench
Crystal structure of human JNK3 complexed with N-{3-cyano-6-[3-(1- PIPERIDINYL)PROPANOYL]-4,5,6,7-TETRAHYDROTHIENO[2,3-C]PYRIDIN-2-yl}- 1-naphthalenecarboxamide
Analyse Crystal structure of human JNK3 complexed with N-{3-cyano-6-[3-(1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O0U
- Type
- protein
- Length
- 331 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
- C0M
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 10 (EC 2.7.11.24) | protein | 331 | 41% helix, 16% strand | P53779 |
Ligands and binding sites
- C0M · N-{3-cyano-6-[3-(1-piperidinyl)propanoyl]-4,5,6,7-tetrahydrothieno[2,3-c]pyridin-2-YL}1-naphthalenecarboxamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 615 | 0.75 | 0.81 | 61 | C0M |
| 2 | 74 | 0.35 | 0.76 | 17 | empty |
| 3 | 56 | 0.28 | 0.75 | 15 | 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 2O0U · PDBe 2O0U · UniProt P53779
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