MolNFT v1 · #111703 · protein
Crystal structure of human PLK4-PB3 in complex with stil-cc
4YYP · SERINE/THREONINE-protein kinase PLK4: “Crystal structure of human PLK4-PB3 in complex with stil-cc”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.42). MolNFT v1 #111703 on GenesisL1: 3D structure, binding sites…
- PDB
- 4YYP
- Type
- protein
- Length
- 119 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase PLK4; Scl-interrupting locus protein
- EC
- 2.7.11.21
- UniProt
- O00444, Q15468
- Ligands
- CL
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase PLK4 (EC 2.7.11.21) | protein | 87 | 18% helix, 37% strand | O00444 |
| B | Scl-interrupting locus protein | protein | 32 | 88% helix, 0% strand | Q15468 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.42 | 0.83 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 960 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4YYP · Crystal structure of human PLK4-PB3 in complex with STIL-CC · the same entry in another collection · chain A against A, TM-score 1.00
- O00444 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase PLK4 (O00444) · a predicted model of the same protein · chain A against A, TM-score 0.88
- Q15468 · AlphaFold monomer V2.0 prediction for scl-interrupting locus protein (Q15468) · a predicted model of the same protein · chain B against A, TM-score 0.79
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
- Every structure of UniProt Q15468
- Elsewhere: RCSB PDB 4YYP · PDBe 4YYP · UniProt O00444 · UniProt Q15468
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