Research workbench
Crystal structure of PLK4 kinase
Analyse Crystal structure of PLK4 kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3COK
- Type
- protein
- Length
- 468 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase PLK4
- EC
- 2.7.11.21
- UniProt
- O00444
- Ligands
- ANP, SO4
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase PLK4 (EC 2.7.11.21) | protein | 234 | 36% helix, 22% strand | O00444 |
| B | SERINE/THREONINE-protein kinase PLK4 (EC 2.7.11.21) | protein | 234 | 37% helix, 22% strand | O00444 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 353 | 0.66 | 0.81 | 35 | ANP |
| 2 | 366 | 0.65 | 0.79 | 38 | ANP |
| 3 | 356 | 0.59 | 0.76 | 45 | SO4 |
| 4 | 236 | 0.58 | 0.79 | 35 | SO4 |
| 5 | 76 | 0.40 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 844 Ų buried · 8 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 O00444
- Elsewhere: RCSB PDB 3COK · PDBe 3COK · UniProt O00444
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