Research workbench
TNNI3K complexed with a 4,6-diaminopyrimidine
Analyse TNNI3K complexed with a 4,6-diaminopyrimidine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B5J
- Type
- protein
- Length
- 1,044 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase TNNI3K
- EC
- 2.7.11.1
- UniProt
- Q59H18
- Ligands
- CV4
- Pockets
- 8 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase TNNI3K (EC 2.7.11.1) | protein | 263 | 44% helix, 18% strand | Q59H18 |
| B | SERINE/THREONINE-protein kinase TNNI3K (EC 2.7.11.1) | protein | 264 | 44% helix, 18% strand | Q59H18 |
| C | SERINE/THREONINE-protein kinase TNNI3K (EC 2.7.11.1) | protein | 260 | 43% helix, 18% strand | Q59H18 |
| D | SERINE/THREONINE-protein kinase TNNI3K (EC 2.7.11.1) | protein | 257 | 41% helix, 19% strand | Q59H18 |
Ligands and binding sites
- CV4 · N-methyl-3-[(6-{[4-(trifluoromethyl) phenyl]amino}pyrimidin-4-yl)amino]benzene-1-sulfonamide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 713 | 0.85 | 0.88 | 86 | empty |
| 2 | 631 | 0.69 | 0.77 | 83 | empty |
| 3 | 55 | 0.69 | 0.97 | 19 | empty |
| 4 | 79 | 0.68 | 0.94 | 25 | empty |
| 5 | 352 | 0.66 | 0.80 | 36 | CV4 |
Interfaces
6 interfaces between chains.
- A–D · 2167 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 2158 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 692 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 399 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 343 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 Q59H18
- Elsewhere: RCSB PDB 6B5J · PDBe 6B5J · UniProt Q59H18
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.