MolNFT v1 · #71557 · protein

14-3-3 sigma in complex with yap PS127-peptide

3MHR · 14-3-3 protein sigma: “14-3-3 sigma in complex with yap PS127-peptide”. X-ray diffraction, 3 ligands (MG, CA, CL). MolNFT v1 #71557 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3MHR
Type: protein
Length: 246 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein sigma; Yap phosphopeptide
UniProt: P31947
Ligands: MG, CA, CL

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	81% helix, 0% strand	P31947
P	Yap phosphopeptide	protein	10	0% helix, 0% strand	—

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains A
CA · Calcium ion · metal · chains A
CL · Chloride ion · ion · 4 copies · chains A
GOL · Glycerol · additive · 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 · 751 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation, phosphorylation).

Compared structures

3MHR · 14-3-3 sigma in complex with YAP pS127-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

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 3MHR · PDBe 3MHR · UniProt P31947

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