MolNFT v1 · #87887 · protein
Crystal structure of aurora a 122-403 C290A, C393A bound to ADP
4CEG · Aurora kinase a: “Crystal structure of aurora a 122-403 C290A, C393A bound to ADP”. X-ray diffraction, 3 ligands (ADP, MG, CL), 1 pocket (best druggability 0.73). MolNFT v1 #87887 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4CEG
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aurora kinase a
- UniProt
- O14965
- Ligands
- ADP, MG, CL
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aurora kinase a | protein | 265 | 41% helix, 19% strand | O14965 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · 4 copies · chains A
- GOL · Glycerol · additive · 2 copies · 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 | 426 | 0.73 | 0.83 | 53 | ADP, MG |
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 4CEG · PDBe 4CEG · UniProt O14965
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