MolNFT v1 · #116096 · protein
Crystal structure of human 14-3-3 gamma in complex with cftr R-domain peptide PS768-PS795
5D3E · 14-3-3 protein gamma: “Crystal structure of human 14-3-3 gamma in complex with cftr R-domain peptide PS768-PS795”. X-ray diffraction, 1 ligand (SEP), 20 pockets (best druggability 0.71). MolNFT v1 #116096 on GenesisL1: 3D structure…
- PDB
- 5D3E
- Type
- protein
- Length
- 1,430 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein gamma; Cystic fibrosis transmembrane conductance regulator
- EC
- 3.6.3.49
- UniProt
- P61981, P13569
- Ligands
- SEP
- Pockets
- 20 · best druggability 0.71
Structure
x-ray diffraction · 7 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, I | 14-3-3 protein gamma | protein | 235 | 82% helix, 0% strand | P61981 |
| B, F | 14-3-3 protein gamma | protein | 238 | 84% helix, 0% strand | P61981 |
| C | Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49) | protein | 11 | 0% helix, 0% strand | P13569 |
| E | 14-3-3 protein gamma | protein | 234 | 81% helix, 0% strand | P61981 |
| G | Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49) | protein | 11 | 0% helix, 0% strand | P13569 |
| J | 14-3-3 protein gamma | protein | 224 | 81% helix, 0% strand | P61981 |
| K | Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49) | protein | 4 | 0% helix, 0% strand | P13569 |
Ligands and binding sites
- SEP · Phosphoserine · ligand · chains J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 365 | 0.71 | 0.83 | 58 | empty |
| 2 | 642 | 0.69 | 0.78 | 66 | empty |
| 3 | 279 | 0.63 | 0.80 | 29 | empty |
| 4 | 268 | 0.60 | 0.79 | 35 | empty |
| 5 | 239 | 0.60 | 0.80 | 28 | empty |
Interfaces
11 interfaces between chains.
- A–B · 1114 Ų buried · 11 hydrogen bonds · protein-protein
- E–F · 1108 Ų buried · 13 hydrogen bonds · protein-protein
- I–J · 1014 Ų buried · 12 hydrogen bonds · protein-protein
- B–F · 929 Ų buried · 14 hydrogen bonds · protein-protein
- A–E · 768 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (phosphorylation).
Compared structures
- 5D3E · Crystal structure of human 14-3-3 gamma in complex with CFTR R-domain peptide pS768-pS795 · the same entry in another collection · chain K against K, 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 I 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 P61981
- Every structure of UniProt P13569
- Elsewhere: RCSB PDB 5D3E · PDBe 5D3E · UniProt P61981 · UniProt P13569
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