Research workbench
14-3-3 sigma in complex with ikappabalpha PS63 peptide
Analyse 14-3-3 sigma in complex with ikappabalpha PS63 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Y1J
- Type
- protein
- Length
- 243 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P31947, P25963
- Ligands
- CA, MG, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 236 | — | P31947 |
| P | — | protein | 7 | — | P25963 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · 7 copies · chains A, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6Y1J · 14-3-3 sigma in complex with IkappaBalpha pS63 peptide · 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 0.95
- P25963 · AlphaFold monomer V2.0 prediction for nf-kappa-B inhibitor alpha (P25963) · a predicted model of the same protein · chain P against A, TM-score 0.52
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 P25963
- Elsewhere: RCSB PDB 6Y1J · PDBe 6Y1J · UniProt P31947 · UniProt P25963
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