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Reduced thiol peroxidase (tpx) from yersinia pseudotuberculosis

Analyse Reduced thiol peroxidase (tpx) from yersinia pseudotuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ZRE
Type
protein
Length
165 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Thiol peroxidase
EC
1.11.1.15
UniProt
Q66A71
Pockets
1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AThiol peroxidase (EC 1.11.1.15)protein16519% helix, 31% strandQ66A71

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1700.450.8218empty

Compared structures

  • 3ZRE · Reduced Thiol peroxidase (Tpx) from yersinia Pseudotuberculosis · the same entry in another collection · chain A against A, TM-score 1.00

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