Research workbench
14-3-3 sigma in complex with phosphorylated SOS1 peptide
Analyse 14-3-3 sigma in complex with phosphorylated SOS1 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Y44
- Type
- protein
- Length
- 236 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; Son of sevenless homolog 1
- UniProt
- P31947, Q07889
- Ligands
- MG, CA, CL
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein sigma | protein | 227 | 81% helix, 0% strand | P31947 |
| P | Son of sevenless homolog 1 | protein | 9 | 0% helix, 0% strand | Q07889 |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–P · 737 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation, phosphorylation).
Compared structures
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
- Every structure of UniProt Q07889
- Elsewhere: RCSB PDB 6Y44 · PDBe 6Y44 · UniProt P31947 · UniProt Q07889
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