Research workbench
Aurora a in complex with YL5-81-1
Analyse Aurora a in complex with YL5-81-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UOK
- Type
- protein
- Length
- 530 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aurora kinase a
- EC
- 2.7.11.1
- UniProt
- O14965
- Ligands
- 0C6
- Pockets
- 4 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aurora kinase a (EC 2.7.11.1) | protein | 265 | 41% helix, 17% strand | O14965 |
Ligands and binding sites
- 0C6 · 4-({4-[(2-chlorophenyl)amino]-5-fluoropyrimidin-2-yl}amino)benzoic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1056 | 0.83 | 0.84 | 90 | empty |
| 2 | 461 | 0.71 | 0.81 | 57 | 0C6 |
| 3 | 254 | 0.68 | 0.84 | 39 | 0C6 |
| 4 | 213 | 0.52 | 0.77 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 1351 Ų buried · 12 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 O14965
- Elsewhere: RCSB PDB 3UOK · PDBe 3UOK · UniProt O14965
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