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Crystal structure of human 14-3-3 gamma in complex with CAMKK2 14-3-3 binding motif SER100 and fusicoccin a
Analyse Crystal structure of human 14-3-3 gamma in complex with CAMKK2 14-3-3 binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Y4K
- Type
- protein
- Length
- 457 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein gamma; CALCIUM/CALMODULIN-dependent protein kinase kinase 2
- EC
- 2.7.11.17
- UniProt
- P61981, Q96RR4
- Ligands
- FSC
- Pockets
- 4 · best druggability 0.52
Structure
x-ray diffraction · 4 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein gamma | protein | 226 | 80% helix, 0% strand | P61981 |
| B | 14-3-3 protein gamma | protein | 216 | 81% helix, 0% strand | P61981 |
| E | CALCIUM/CALMODULIN-dependent protein kinase kinase 2 (EC 2.7.11.17) | protein | 8 | 0% helix, 0% strand | Q96RR4 |
| F | CALCIUM/CALMODULIN-dependent protein kinase kinase 2 (EC 2.7.11.17) | protein | 7 | 0% helix, 0% strand | Q96RR4 |
Ligands and binding sites
- FSC · Fusicoccin · ligand · chains A, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 184 | 0.52 | 0.78 | 22 | FSC |
| 2 | 308 | 0.52 | 0.74 | 38 | empty |
| 3 | 79 | 0.48 | 0.83 | 16 | empty |
| 4 | 74 | 0.45 | 0.81 | 14 | empty |
Interfaces
3 interfaces between chains.
- A–B · 933 Ų buried · 8 hydrogen bonds · protein-protein
- B–F · 525 Ų buried · 12 hydrogen bonds · protein-protein
- A–E · 505 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 6Y4K · Crystal structure of human 14-3-3 gamma in complex with CaMKK2 14-3-3 binding motif… · the same entry in another collection · chain F against F, 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 A 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 E against A, TM-score 0.47
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 6Y4K · PDBe 6Y4K · UniProt P61981 · UniProt Q96RR4
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