Research workbench
TNNI3K complexed with inhibitor 2
Analyse TNNI3K complexed with inhibitor 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YFF
- Type
- protein
- Length
- 1,043 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
- 4CV
- Pockets
- 9 · best druggability 0.70
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 | 264 | 42% helix, 18% strand | Q59H18 |
| B | SERINE/THREONINE-protein kinase TNNI3K (EC 2.7.11.1) | protein | 264 | 42% helix, 18% strand | Q59H18 |
| C | SERINE/THREONINE-protein kinase TNNI3K (EC 2.7.11.1) | protein | 258 | 44% helix, 18% strand | Q59H18 |
| D | SERINE/THREONINE-protein kinase TNNI3K (EC 2.7.11.1) | protein | 257 | 44% helix, 18% strand | Q59H18 |
Ligands and binding sites
- 4CV · 3-[(5-bromo-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]-N-methyl-4-(morpholin-4-yl)benzenesulfonamide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.70 | 0.97 | 19 | empty |
| 2 | 58 | 0.69 | 0.97 | 18 | empty |
| 3 | 396 | 0.68 | 0.81 | 42 | 4CV |
| 4 | 397 | 0.67 | 0.80 | 39 | 4CV |
| 5 | 259 | 0.67 | 0.83 | 26 | 4CV |
Interfaces
3 interfaces between chains.
- B–C · 2134 Ų buried · 21 hydrogen bonds · protein-protein
- A–D · 2089 Ų buried · 24 hydrogen bonds · protein-protein
- C–D · 563 Ų buried · 7 hydrogen bonds · 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 4YFF · PDBe 4YFF · UniProt Q59H18
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