MolNFT v1 · #184040 · protein
Crystal structure of 14-3-3 sigma in complex with NPM1 phosphopeptide and stabilizer fusicoccin-a
7OBH · 14-3-3 protein sigma: “Crystal structure of 14-3-3 sigma in complex with NPM1 phosphopeptide and stabilizer fusicoccin-a”. X-ray diffraction, 2 ligands (FSC, CL), 1 pocket (best druggability 0.57). MolNFT v1 #184040 on GenesisL1: 3D…
- PDB
- 7OBH
- 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; NPM1 phosphopeptide
- UniProt
- P31947, P06748
- Ligands
- FSC, CL
- Pockets
- 1 · best druggability 0.57
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 | NPM1 phosphopeptide | protein | 6 | 0% helix, 0% strand | P06748 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.57 | 0.82 | 16 | FSC |
Interfaces
1 interface between chains.
- A–B · 574 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation, phosphorylation).
Compared structures
- 7OBH · Crystal structure of 14-3-3 sigma in complex with NPM1 phosphopeptide and stabilizer… · 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
- P06748 · AlphaFold monomer V2.0 prediction for nucleophosmin (P06748) · a predicted model of the same protein · chain B against A, TM-score 0.61
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 P06748
- Elsewhere: RCSB PDB 7OBH · PDBe 7OBH · UniProt P31947 · UniProt P06748
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