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Crystal structure of human 14-3-3 sigma C38V/N166H in complex with task-3 peptide and stabilizer Fc-thf
Analyse Crystal structure of human 14-3-3 sigma C38V/N166H in complex with task-3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SPR
- Type
- protein
- Length
- 242 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; Task-3 peptide
- UniProt
- P31947
- Ligands
- FC7, MG, CL
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein sigma | protein | 236 | 79% helix, 0% strand | P31947 |
| P | Task-3 peptide | protein | 6 | 0% helix, 0% strand | — |
Ligands and binding sites
- FC7 · Fusicoccin A-THF · ligand · chains A, P
- MG · Magnesium ion · metal · 3 copies · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.45 | 0.77 | 22 | FC7 |
Interfaces
1 interface between chains.
- A–P · 504 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 3SPR · Crystal structure of human 14-3-3 sigma C38V/N166H in complex with TASK-3 peptide and… · the same entry in another collection · chain A against A, TM-score 1.00
- P31947 · AlphaFold monomer V2.0 prediction for 14-3-3 protein sigma (P31947) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P31947
- Elsewhere: RCSB PDB 3SPR · PDBe 3SPR · UniProt P31947
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