Research workbench
Crystal structure of 14-3-3 sigma in complex with RIPK2 phosphopeptide
Analyse Crystal structure of 14-3-3 sigma in complex with RIPK2 phosphopeptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OBS
- 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; Receptor-interacting SERINE/THREONINE-protein kinase 2
- EC
- 2.7.11.1, 2.7.10.2
- UniProt
- P31947, O43353
- Ligands
- MG, CA
- Pockets
- 2 · best druggability 0.51
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 | 236 | 80% helix, 0% strand | P31947 |
| B | Receptor-interacting SERINE/THREONINE-protein kinase 2 (EC 2.7.11.1, 2.7.10.2) | protein | 6 | 0% helix, 0% strand | O43353 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.51 | 0.83 | 18 | empty |
| 2 | 69 | 0.34 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 575 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation, phosphorylation).
Compared structures
- 7OBS · Crystal structure of 14-3-3 sigma in complex with RIPK2 phosphopeptide · 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
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 O43353
- Elsewhere: RCSB PDB 7OBS · PDBe 7OBS · UniProt P31947 · UniProt O43353
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