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14-3-3 sigma in complex with taz PS89 peptide and fragment NV2

Analyse 14-3-3 sigma in complex with taz PS89 peptide and fragment NV2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5N5T
Type: protein
Length: 236 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein sigma; Taz PS89 peptide
UniProt: P31947
Ligands: 8OB, MG, CL

Structure

x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein sigma	protein	228	82% helix, 0% strand	P31947
P	Taz PS89 peptide	protein	8	0% helix, 0% strand	—

Ligands and binding sites

8OB · 4-[3,5-bis(chloranyl)pyridin-2-yl]oxyphenol · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · chains A

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

Interfaces

1 interface between chains.

A–P · 679 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

5N5T · 14-3-3 sigma in complex with TAZ pS89 peptide and fragment NV2 · 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 0.96

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 5N5T · PDBe 5N5T · UniProt P31947

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