Research workbench
Crystal structure of 14-3-3 gamma
Analyse Crystal structure of 14-3-3 gamma in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UZD
- Type
- protein
- Length
- 238 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein gamma; Histone deacetylase 4
- EC
- 3.5.1.98
- UniProt
- P61981, P56524
- Ligands
- MG, NO3
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein gamma | protein | 229 | 83% helix, 0% strand | P61981 |
| B | Histone deacetylase 4 (EC 3.5.1.98) | protein | 9 | 0% helix, 0% strand | P56524 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 207 | 0.60 | 0.81 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 613 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 3UZD · Crystal structure of 14-3-3 GAMMA · the same entry in another collection · chain A against A, 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
- P56524 · AlphaFold monomer V2.0 prediction for histone deacetylase 4 (P56524) · a predicted model of the same protein · chain B against A, TM-score 0.46
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 P56524
- Elsewhere: RCSB PDB 3UZD · PDBe 3UZD · UniProt P61981 · UniProt P56524
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