Research workbench
Crystal structure of the human BUB1 kinase domain in complex with bay 1816032
Analyse Crystal structure of the human BUB1 kinase domain in complex with bay 1816032 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F7B
- Type
- protein
- Length
- 343 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O43683
- Ligands
- CVQ, MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 343 | — | O43683 |
Ligands and binding sites
- CVQ · 2-[3,5-bis(fluoranyl)-4-[[3-[5-methoxy-4-[(3-methoxypyridin-4-yl)amino]pyrimidin-2-yl]indazol-1-yl]methyl]phenoxy]ethanol · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6F7B · Crystal structure of the human Bub1 kinase domain in complex with BAY 1816032 · the same entry in another collection · chain A against A, TM-score 1.00
- O43683 · AlphaFold monomer V2.0 prediction for mitotic checkpoint SERINE/THREONINE-protein kinase… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O43683
- Elsewhere: RCSB PDB 6F7B · PDBe 6F7B · UniProt O43683
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