Research workbench
Aurora a kinase in complex with 2-(3-FLUOROPHENYL)QUINOLINE-4- carboxylic acid and ATP
Analyse Aurora a kinase in complex with 2-(3-FLUOROPHENYL)QUINOLINE-4- carboxylic acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OBJ
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aurora kinase a
- EC
- 2.7.11.1
- UniProt
- O14965
- Ligands
- ATP, 9QK, MG, SO4
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aurora kinase a (EC 2.7.11.1) | protein | 260 | 42% helix, 20% strand | O14965 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- 9QK · 2-(3-fluorophenyl)quinoline-4-carboxylic acid · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.72 | 0.82 | 44 | MG, ATP |
| 2 | 113 | 0.42 | 0.77 | 18 | empty |
| 3 | 86 | 0.42 | 0.78 | 13 | 9QK |
Compared structures
- 5OBJ · Aurora A kinase in complex with 2-(3-fluorophenyl)quinoline-4-carboxylic acid and ATP · the same entry in another collection · chain A against A, TM-score 1.00
- O14965 · AlphaFold monomer V2.0 prediction for aurora kinase a (O14965) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 5OBJ · PDBe 5OBJ · UniProt O14965
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