Research workbench
Recognition of an intrachain tandem 14-3-3 binding site within protein kinase C epsilon
Analyse Recognition of an intrachain tandem 14-3-3 binding site within protein kinase C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WH0
- Type
- protein
- Length
- 918 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein ZETA/DELTA; Protein kinase C epsilon type, npkc-epsilon
- EC
- 2.7.11.13
- UniProt
- P63104, Q02156
- Ligands
- CA
- Pockets
- 9 · best druggability 0.62
Structure
x-ray diffraction · 6 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein ZETA/DELTA | protein | 221 | 85% helix, 0% strand | P63104 |
| B | 14-3-3 protein ZETA/DELTA | protein | 227 | 83% helix, 0% strand | P63104 |
| C | 14-3-3 protein ZETA/DELTA | protein | 226 | 80% helix, 0% strand | P63104 |
| D | 14-3-3 protein ZETA/DELTA | protein | 222 | 80% helix, 0% strand | P63104 |
| Q | Protein kinase C epsilon type, npkc-epsilon (EC 2.7.11.13) | protein | 13 | 0% helix, 0% strand | Q02156 |
| R | Protein kinase C epsilon type, npkc-epsilon (EC 2.7.11.13) | protein | 9 | 0% helix, 0% strand | Q02156 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 144 | 0.62 | 0.86 | 26 | empty |
| 2 | 432 | 0.60 | 0.75 | 36 | empty |
| 3 | 192 | 0.55 | 0.79 | 24 | empty |
| 4 | 304 | 0.53 | 0.75 | 26 | empty |
| 5 | 179 | 0.51 | 0.77 | 23 | empty |
Interfaces
7 interfaces between chains.
- A–B · 876 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 750 Ų buried · 10 hydrogen bonds · protein-protein
- B–Q · 547 Ų buried · 10 hydrogen bonds · protein-protein
- A–Q · 427 Ų buried · 13 hydrogen bonds · protein-protein
- D–R · 374 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 2WH0 · Recognition of an intrachain tandem 14-3-3 binding site within protein kinase C epsilon · the same entry in another collection · chain R against R, 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 B against A, TM-score 0.99
- Q02156 · AlphaFold monomer V2.0 prediction for protein kinase C epsilon type (Q02156) · a predicted model of the same protein · chain R against A, TM-score 0.54
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 Q02156
- Elsewhere: RCSB PDB 2WH0 · PDBe 2WH0 · UniProt P63104 · UniProt Q02156
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