MolNFT v1 · #151949 · protein
Aurora-a kinase domain in complex with coenzyme a
6I2U · Aurora kinase a: “Aurora-a kinase domain in complex with coenzyme a”. X-ray diffraction, 2 ligands (COA, MG), 1 pocket (best druggability 0.71). MolNFT v1 #151949 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6I2U
- Type
- protein
- Length
- 265 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
- COA, MG
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aurora kinase a (EC 2.7.11.1) | protein | 265 | 39% helix, 20% strand | O14965 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A
- MG · Magnesium ion · metal · 4 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 3 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 | 549 | 0.71 | 0.80 | 56 | COA, MG |
Modifications
Observed in the structure: 3 covalent, 2 modified (additive adduct, phosphorylation, covalent ligand).
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 6I2U · PDBe 6I2U · UniProt O14965
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