MolNFT v1 · #127791 · protein

14-3-3 sigma in complex with taz PS89 peptide

5N75 · 14-3-3 protein sigma: “14-3-3 sigma in complex with taz PS89 peptide”. X-ray diffraction, 2 ligands (MG, CL). MolNFT v1 #127791 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5N75
Type: protein
Length: 244 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein sigma; Ww domain-containing transcription regulator protein 1
UniProt: P31947, C9JQS8
Ligands: MG, CL

Structure

x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein sigma	protein	234	80% helix, 0% strand	P31947
P	Ww domain-containing transcription regulator protein 1	protein	10	0% helix, 0% strand	C9JQS8

Ligands and binding sites

MG · Magnesium ion · metal · 3 copies · chains A, P
CL · Chloride ion · ion · 3 copies · chains A

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

Interfaces

1 interface between chains.

A–P · 827 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

5N75 · 14-3-3 sigma in complex with TAZ pS89 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 0.96

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
Every structure of UniProt C9JQS8
Elsewhere: RCSB PDB 5N75 · PDBe 5N75 · UniProt P31947 · UniProt C9JQS8

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