Research workbench
Structure of dephosphorylated aurora a (122-403) in complex with inhibiting monobody and AT9283 in an inactive conformation
Analyse Structure of dephosphorylated aurora a (122-403) in complex with inhibiting… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CPG
- Type
- protein
- Length
- 678 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O14965
- Ligands
- 35R
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 249 | — | O14965 |
| B | — | protein | 89 | — | — |
| D | — | protein | 252 | — | O14965 |
| E | — | protein | 88 | — | — |
Ligands and binding sites
- 35R · 1-cyclopropyl-3-{3-[5-(morpholin-4-ylmethyl)-1H-benzimidazol-2-yl]-1H-pyrazol-4-yl}urea · ligand · 2 copies · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- O14965 · AlphaFold monomer V2.0 prediction for aurora kinase a (O14965) · a predicted model of the same protein · chain D against A, TM-score 0.95
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 6CPG · PDBe 6CPG · UniProt O14965
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