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Reduced sweetness of a monellin (mnei) mutant results from increased protein flexibility and disruption of a distant poly-(L-proline) II helix

Analyse Reduced sweetness of a monellin (mnei) mutant results from increased protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PYJ
Type: protein
Length: 96 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Monellin chain B/MONELLIN chain a chimeric protein
UniProt: P02882, P02881

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Monellin chain B/MONELLIN chain a chimeric protein	protein	96	18% helix, 55% strand	P02882, P02881

Ligands and binding sites

FMT · Formic acid · additive · chains A

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

Compared structures

3PYJ · Reduced sweetness of a monellin (MNEI) mutant results from increased protein flexibility… · the same entry in another collection · chain A against A, TM-score 1.00
P02882 · AlphaFold monomer V2.0 prediction for monellin chain B (P02882) · a predicted model of the same protein · chain A against A, TM-score 0.48
P02881 · AlphaFold monomer V2.0 prediction for monellin chain a (P02881) · a predicted model of the same protein · chain A against A, TM-score 0.45

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 P02882
Every structure of UniProt P02881
Elsewhere: RCSB PDB 3PYJ · PDBe 3PYJ · UniProt P02882 · UniProt P02881

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