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Molecular tweezers modulate 14-3-3 protein-protein interactions

Analyse Molecular tweezers modulate 14-3-3 protein-protein interactions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OEG
Type: protein
Length: 228 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein sigma
UniProt: P31947
Ligands: 9SZ, CL
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein sigma	protein	228	80% helix, 0% strand	P31947

Ligands and binding sites

9SZ · C42 H32 O8 P2 · ligand · chains A
CL · Chloride ion · ion · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	301	0.53	0.74	31	empty
2	66	0.38	0.79	19	empty

Compared structures

5OEG · Molecular tweezers modulate 14-3-3 protein-protein interactions · 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
Elsewhere: RCSB PDB 5OEG · PDBe 5OEG · UniProt P31947

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