Research workbench
Crystal structure of aurora-a kinase in complex with N-myc
Analyse Crystal structure of aurora-a kinase in complex with N-myc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5G1X
- Type
- protein
- Length
- 292 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aurora kinase a; N-myc proto-oncogene protein
- EC
- 2.7.11.1
- UniProt
- O14965, P04198
- Ligands
- ADP, MG
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aurora kinase a (EC 2.7.11.1) | protein | 263 | 41% helix, 19% strand | O14965 |
| B | N-myc proto-oncogene protein | protein | 29 | 55% helix, 0% strand | P04198 |
Ligands and binding sites
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 | 546 | 0.74 | 0.82 | 64 | ADP, MG |
Interfaces
1 interface between chains.
- A–B · 1038 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 5G1X · Crystal structure of Aurora-A kinase in complex with N-Myc · the same entry in another collection · chain A against A, TM-score 1.00
- O14965 · AlphaFold monomer V2.0 prediction for aurora kinase a (O14965) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P04198 · AlphaFold monomer V2.0 prediction for N-myc proto-oncogene protein (P04198) · a predicted model of the same protein · chain B against A, TM-score 0.50
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
- Every structure of UniProt P04198
- Elsewhere: RCSB PDB 5G1X · PDBe 5G1X · UniProt O14965 · UniProt P04198
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