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Two crystal structures of a potently sweet protein: natural monellin at 2.75 ångströms resolution and single-chain monellin at 1.7 ångströms resolution

Analyse Two crystal structures of a potently sweet protein: natural monellin at 2.75… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1MOL
Type
protein
Length
188 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Monellin
UniProt
P02882
Pockets
1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMonellinprotein9418% helix, 53% strandP02882

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13070.620.7936empty

Interfaces

1 interface between chains.

  • A–B · 559 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 1MOL · Two crystal structures of a potently sweet protein: natural monellin at 2.75 ångströms… · 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 0.50

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