Research workbench
Phosphorylation independent interactions between 14-3-3 and exoenzyme S: from structure to pathogenesis
Analyse Phosphorylation independent interactions between 14-3-3 and exoenzyme S: from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O02
- Type
- protein
- Length
- 478 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein ZETA/DELTA; Exos (416-430) peptide
- UniProt
- P63104
- Ligands
- BEZ
- Pockets
- 4 · best druggability 0.51
Structure
x-ray diffraction · 4 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein ZETA/DELTA | protein | 224 | 84% helix, 0% strand | P63104 |
| B | 14-3-3 protein ZETA/DELTA | protein | 230 | 83% helix, 0% strand | P63104 |
| P | Exos (416-430) peptide | protein | 14 | 29% helix, 0% strand | — |
| Q | Exos (416-430) peptide | protein | 10 | 40% helix, 0% strand | — |
Ligands and binding sites
- BEZ · Benzoic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 300 | 0.51 | 0.74 | 26 | empty |
| 2 | 59 | 0.34 | 0.77 | 15 | empty |
| 3 | 53 | 0.27 | 0.74 | 17 | empty |
| 4 | 51 | 0.24 | 0.73 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1008 Ų buried · 12 hydrogen bonds · protein-protein
- A–P · 939 Ų buried · 20 hydrogen bonds · protein-protein
- B–Q · 694 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2O02 · Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure… · the same entry in another collection · chain B against B, 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
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
- Elsewhere: RCSB PDB 2O02 · PDBe 2O02 · UniProt P63104
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