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14-3-3 sigma in complex with phosphorylated C-jun peptide

Analyse 14-3-3 sigma in complex with phosphorylated C-jun peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6Y3V
Type
protein
Length
235 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
14-3-3 protein sigma
UniProt
P31947
Ligands
SEP, MG, CA
Pockets
1 · best druggability 0.43

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A14-3-3 protein sigmaprotein23580% helix, 0% strandP31947

Ligands and binding sites

  • SEP · Phosphoserine · ligand · chains A
  • MG · Magnesium ion · metal · 2 copies · chains A
  • CA · Calcium ion · metal · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11510.430.7423SEP

Compared structures

  • 6Y3V · 14-3-3 Sigma in complex with phosphorylated c-Jun 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

Analyse

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