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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
3PXM
Type
protein
Length
192 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Monellin chain B/MONELLIN chain a chimeric protein
UniProt
P02882, P02881
Pockets
1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMonellin chain B/MONELLIN chain a chimeric proteinprotein9618% helix, 50% strandP02882, P02881

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11980.500.7725empty

Interfaces

1 interface between chains.

  • A–B · 585 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 3PXM · 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 0.44

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