MolNFT v1 · #81384 · protein
Aurora a in complex with RPM1686
3UP2 · Aurora kinase a: “Aurora a in complex with RPM1686”. X-ray diffraction, 1 ligand (0C8), 2 pockets (best druggability 0.72). MolNFT v1 #81384 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3UP2
- 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
- 0C8
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 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
- 0C8 · 4-[(4-{[2-(trifluoromethoxy)phenyl]amino}pyrimidin-2-yl)amino]benzoic acid · ligand · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 408 | 0.72 | 0.83 | 54 | 0C8 |
| 2 | 58 | 0.33 | 0.76 | 12 | EDO |
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 3UP2 · PDBe 3UP2 · UniProt O14965
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