Research workbench
Stil binding to the polo-box domain 3 of PLK4 regulates centriole duplication
Analyse Stil binding to the polo-box domain 3 of PLK4 regulates centriole duplication in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N19
- Type
- protein
- Length
- 88 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase PLK4
- EC
- 2.7.11.21
- UniProt
- O00444
- Pockets
- 1 · best druggability 0.47
Structure
solution nmr · 1 distinct chain · 17% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase PLK4 (EC 2.7.11.21) | protein | 88 | 17% helix, 34% strand | O00444 |
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 | 183 | 0.47 | 0.75 | 24 | empty |
Compared structures
- 2N19 · STIL binding to the Polo-box domain 3 of PLK4 regulates centriole duplication · 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 0.69
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 2N19 · PDBe 2N19 · UniProt O00444
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