Crystal structure of human 14-3-3 gamma in complex with CAMKK2 14-3-3 binding motif SER100 and 16-ome-fusicoccin H

Structure

x-ray diffraction · 4 distinct chains · 76% helix, 0% strand (DSSP).

Ligands and binding sites

• OD8 · (2~{R},3~{S},4~{S},5~{R},6~{S})-2-(hydroxymethyl)-6-[[(1~{S},3~{R},6~{S},7~{S},8~{R},9~{R},10~{R},11~{R}, 14~{S})-14-(me thoxymethyl)-3,10-dimethyl-9-oxidanyl-6-propan-2-yl-8-tricyclo[9.3.0.0^{3, 7}]tetradecanyl]oxy]oxane-3,4,5-triol · ligand · chains B, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• A–B · 980 Ų buried · 10 hydrogen bonds · protein-protein
• A–C · 553 Ų buried · 14 hydrogen bonds · protein-protein
• B–D · 505 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

• 6Y6B · Crystal structure of human 14-3-3 gamma in complex with CaMKK2 14-3-3 binding motif… · the same entry in another collection · chain D against D, TM-score 1.00
• P61981 · AlphaFold monomer V2.0 prediction for 14-3-3 protein gamma (P61981) · a predicted model of the same protein · chain B against A, TM-score 0.99
• Q96RR4 · AlphaFold monomer V2.0 prediction for CALCIUM/CALMODULIN-dependent protein kinase kinase… · a predicted model of the same protein · chain C 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 P61981
• Every structure of UniProt Q96RR4
• Elsewhere: RCSB PDB 6Y6B · PDBe 6Y6B · UniProt P61981 · UniProt Q96RR4