Research workbench
Aurora A in complex with RPM1680
Analyse Aurora A in complex with RPM1680 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UO4
- Type
- protein
- Length
- 266 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.45
- Source
- Homo sapiens
- Molecule
- Aurora kinase A
- EC
- 2.7.11.1
- UniProt
- O14965
- Ligands
- 0C0
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · resolution 2.45 · 1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aurora kinase A (EC 2.7.11.1) | protein | 266 | 39% helix, 17% strand | O14965 |
Ligands and binding sites
- 0C0 · 4-{[4-(biphenyl-2-ylamino)pyrimidin-2-yl]amino}benzoic acid · ligand · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.64 | 0.81 | 27 | 0C0 |
| 2 | 53 | 0.57 | 0.91 | 23 | empty |
| 3 | 120 | 0.49 | 0.80 | 20 | empty |
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 3UO4 · PDBe 3UO4 · UniProt O14965
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