MolNFT v1 · #17186 · protein
Structure of human aurora-a 122-403 phosphorylated on THR287, THR288
1OL7 · SERINE/THREONINE kinase 6: “Structure of human aurora-a 122-403 phosphorylated on THR287, THR288”. X-ray diffraction, 2 ligands (ADP, MG), 2 pockets (best druggability 0.73). MolNFT v1 #17186 on GenesisL1: 3D structure, binding…
- PDB
- 1OL7
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE kinase 6
- EC
- 2.7.1.37
- UniProt
- O14965
- Ligands
- ADP, MG
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE kinase 6 (EC 2.7.1.37) | protein | 263 | 40% helix, 19% strand | O14965 |
Ligands and binding sites
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 | 514 | 0.73 | 0.81 | 62 | ADP, MG |
| 2 | 60 | 0.30 | 0.74 | 13 | empty |
Modifications
Observed in the structure: 2 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 1OL7 · PDBe 1OL7 · UniProt O14965
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