Research workbench
Structure of the MST4 and 14-3-3 complex
Analyse Structure of the MST4 and 14-3-3 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XY9
- Type
- protein
- Length
- 482 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein ZETA/DELTA; Peptide from SERINE/THREONINE-protein kinase 26
- EC
- 2.7.11.1
- UniProt
- P63104, Q9P289
- Pockets
- 6 · best druggability 0.60
Structure
x-ray diffraction · 3 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein ZETA/DELTA | protein | 232 | 82% helix, 0% strand | P63104 |
| B | 14-3-3 protein ZETA/DELTA | protein | 230 | 83% helix, 0% strand | P63104 |
| C, D | Peptide from SERINE/THREONINE-protein kinase 26 (EC 2.7.11.1) | protein | 10 | 0% helix, 0% strand | Q9P289 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
- PE4 · 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol · additive · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 175 | 0.60 | 0.83 | 31 | PE4 |
| 2 | 369 | 0.55 | 0.75 | 30 | empty |
| 3 | 163 | 0.54 | 0.80 | 26 | empty |
| 4 | 90 | 0.39 | 0.77 | 21 | empty |
| 5 | 95 | 0.38 | 0.76 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 883 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 703 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 688 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 5XY9 · Structure of the MST4 and 14-3-3 complex · the same entry in another collection · chain A against A, TM-score 1.00
- P63104 · AlphaFold monomer V2.0 prediction for 14-3-3 protein ZETA/DELTA (P63104) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q9P289 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase 26 (Q9P289) · a predicted model of the same protein · chain C against A, TM-score 0.41
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 P63104
- Every structure of UniProt Q9P289
- Elsewhere: RCSB PDB 5XY9 · PDBe 5XY9 · UniProt P63104 · UniProt Q9P289
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