Research workbench
Aurora a in complex with RPM1693
Analyse Aurora a in complex with RPM1693 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UOD
- Type
- protein
- Length
- 266 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
- 0C3
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aurora kinase a (EC 2.7.11.1) | protein | 266 | 40% helix, 19% strand | O14965 |
Ligands and binding sites
- 0C3 · 4-[(4-{[2-(trifluoromethyl)phenyl]amino}pyrimidin-2-yl)amino]benzoic acid · ligand · chains A
- EDO · 1,2-ethanediol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · 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 | 425 | 0.70 | 0.81 | 43 | 0C3 |
| 2 | 58 | 0.36 | 0.78 | 15 | empty |
| 3 | 54 | 0.28 | 0.74 | 14 | 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 3UOD · PDBe 3UOD · UniProt O14965
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