Research workbench
Crystal structure of human 14-3-3 zeta in complex with cftr R-domain peptide PS753-PS768 and stabilizer fusicoccin-a
Analyse Crystal structure of human 14-3-3 zeta in complex with cftr R-domain peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5D3F
- Type
- protein
- Length
- 463 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein ZETA/DELTA; Cystic fibrosis transmembrane conductance regulator
- EC
- 3.6.3.49
- UniProt
- P63104, P13569
- Ligands
- FSC
- Pockets
- 6 · best druggability 0.65
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 | 221 | 84% helix, 0% strand | P63104 |
| B | 14-3-3 protein ZETA/DELTA | protein | 224 | 84% helix, 0% strand | P63104 |
| C | Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49) | protein | 18 | 0% helix, 0% strand | P13569 |
Ligands and binding sites
- FSC · Fusicoccin · ligand · chains B, 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 437 | 0.65 | 0.78 | 49 | FSC |
| 2 | 223 | 0.58 | 0.80 | 36 | empty |
| 3 | 149 | 0.46 | 0.76 | 22 | empty |
| 4 | 95 | 0.36 | 0.74 | 14 | empty |
| 5 | 61 | 0.30 | 0.75 | 14 | empty |
Interfaces
3 interfaces between chains.
- A–C · 863 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 795 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 550 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 5D3F · Crystal structure of human 14-3-3 zeta in complex with CFTR R-domain peptide pS753-pS768… · 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 0.98
- P13569 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain C against A, TM-score 0.23
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 P13569
- Elsewhere: RCSB PDB 5D3F · PDBe 5D3F · UniProt P63104 · UniProt P13569
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