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Structure of human aurora a in complex with a diaminopyrimidine
Analyse Structure of human aurora a in complex with a diaminopyrimidine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QBN
- Type
- protein
- Length
- 250 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase 6
- EC
- 2.7.11.1
- UniProt
- O14965
- Ligands
- E9Z
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase 6 (EC 2.7.11.1) | protein | 250 | 39% helix, 18% strand | O14965 |
Ligands and binding sites
- E9Z · 5-chloro-N~4~-cyclopropyl-N~2~-[4-(2-methoxyethoxy)phenyl]pyrimidine-2,4-diamine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 630 | 0.72 | 0.79 | 48 | E9Z |
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 3QBN · PDBe 3QBN · UniProt O14965
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