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The structures of three crystal forms of the sweet protein thaumatin

Analyse The structures of three crystal forms of the sweet protein thaumatin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1THU
Type
protein
Length
207 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Thaumatin isoform B
UniProt
P02883
Pockets
1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AThaumatin isoform Bprotein20710% helix, 34% strandP02883

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1630.500.8522empty

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 1THU · The structures of three crystal forms of the sweet protein thaumatin · the same entry in another collection · chain A against A, TM-score 1.00

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