MolNFT v1 · #116935 · protein
Aurora a kinase in complex with ATP in space group P6122
5DT3 · Aurora kinase a: “Aurora a kinase in complex with ATP in space group P6122”. X-ray diffraction, 3 ligands (ATP, MG, SO4), 2 pockets (best druggability 0.76). MolNFT v1 #116935 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5DT3
- Type
- protein
- Length
- 264 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
- ATP, MG, SO4
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aurora kinase a (EC 2.7.11.1) | protein | 264 | 42% helix, 20% strand | O14965 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · 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 | 503 | 0.76 | 0.84 | 54 | MG, ATP |
| 2 | 67 | 0.34 | 0.76 | 13 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
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 5DT3 · PDBe 5DT3 · UniProt O14965
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