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Thaumatin-like protein of amycolatopsis rifamycinica

Analyse Thaumatin-like protein of amycolatopsis rifamycinica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7P22
Type
protein
Length
441 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Thaumatin pathogenesis-like protein
UniProt
A0A066TYR3
Pockets
3 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AThaumatin pathogenesis-like proteinprotein2218% helix, 34% strandA0A066TYR3
BThaumatin pathogenesis-like proteinprotein2208% helix, 35% strandA0A066TYR3

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11530.440.7629empty
2920.400.7719empty
3500.250.7312empty

Interfaces

1 interface between chains.

  • A–B · 452 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

  • 7P22 · Thaumatin-like protein of Amycolatopsis rifamycinica · the same entry in another collection · chain A against A, TM-score 1.00

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