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Crystal structure of the human CAMKK2B
Analyse Crystal structure of the human CAMKK2B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UY6
- Type
- protein
- Length
- 282 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
- 8R4
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CALCIUM/CALMODULIN-dependent protein kinase kinase 2 (EC 2.7.11.17) | protein | 282 | 33% helix, 20% strand | Q96RR4 |
Ligands and binding sites
- 8R4 · 2-cyclopentyl-4-(5-phenylfuro[2,3-b]pyridin-3-yl) benzoic acid · ligand · 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 | 202 | 0.70 | 0.87 | 26 | 8R4 |
| 2 | 111 | 0.44 | 0.78 | 18 | empty |
| 3 | 63 | 0.33 | 0.76 | 16 | empty |
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 Q96RR4
- Elsewhere: RCSB PDB 5UY6 · PDBe 5UY6 · UniProt Q96RR4
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