Research workbench
Aurora A Kinase in complex with ATP in space group P41212
Analyse Aurora A Kinase in complex with ATP in space group P41212 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DNR
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.95
- Source
- Homo sapiens
- Molecule
- Aurora kinase A
- EC
- 2.7.11.1
- UniProt
- O14965
- Ligands
- ATP, MG, SO4
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · resolution 1.95 · 1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aurora kinase A (EC 2.7.11.1) | protein | 265 | 41% helix, 20% strand | O14965 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · 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 | 438 | 0.75 | 0.84 | 43 | MG, ATP |
| 2 | 66 | 0.32 | 0.75 | 13 | empty |
| 3 | 50 | 0.28 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
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 5DNR · PDBe 5DNR · UniProt O14965
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