Research workbench
Crystal structure of the human CAMKK2B in complex with BI2526
Analyse Crystal structure of the human CAMKK2B in complex with BI2526 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BQQ
- Type
- protein
- Length
- 271 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CALCIUM/CALMODULIN-dependent protein kinase kinase 2
- EC
- 2.7.11.17
- UniProt
- Q96RR4
- Ligands
- R78
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CALCIUM/CALMODULIN-dependent protein kinase kinase 2 (EC 2.7.11.17) | protein | 271 | 34% helix, 21% strand | Q96RR4 |
Ligands and binding sites
- R78 · 4-{[(7R)-8-cyclopentyl-7-ethyl-5-methyl-6-oxo-5,6,7,8-tetrahydropteridin-2-yl]amino}-3-methoxy-N-(1-methylpiperidin-4-yl)benzamide · ligand · chains A
- ACT · Acetate ion · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 372 | 0.65 | 0.79 | 38 | R78 |
| 2 | 103 | 0.38 | 0.75 | 19 | ACT |
| 3 | 55 | 0.28 | 0.74 | 15 | empty |
Compared structures
- 6BQQ · Crystal Structure of the Human CAMKK2B in complex with BI2526 · the same entry in another collection · chain A against A, TM-score 1.00
- Q96RR4 · AlphaFold monomer V2.0 prediction for CALCIUM/CALMODULIN-dependent protein kinase 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 Q96RR4
- Elsewhere: RCSB PDB 6BQQ · PDBe 6BQQ · UniProt Q96RR4
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