Research workbench
Crystal structure of aurora-2, an oncogenic serine- threonine kinase
Analyse Crystal structure of aurora-2, an oncogenic serine- threonine kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MUO
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aurora-related kinase 1
- UniProt
- O14965
- Ligands
- ADN
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aurora-related kinase 1 | protein | 251 | 36% helix, 12% strand | O14965 |
Ligands and binding sites
- ADN · Adenosine · ligand · 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 | 254 | 0.62 | 0.80 | 32 | ADN |
| 2 | 90 | 0.36 | 0.75 | 17 | empty |
| 3 | 68 | 0.29 | 0.73 | 11 | 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 1MUO · PDBe 1MUO · UniProt O14965
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