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T391A precursor mutant protein of gamma-glutamyltranspeptidase from escherichia COLI

Analyse T391A precursor mutant protein of gamma-glutamyltranspeptidase from escherichia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2E0W
Type
protein
Length
996 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gamma-glutamyltranspeptidase
EC
2.3.2.2
UniProt
P18956
Pockets
6 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGamma-glutamyltranspeptidase (EC 2.3.2.2)protein49639% helix, 19% strandP18956
BGamma-glutamyltranspeptidase (EC 2.3.2.2)protein50039% helix, 18% strandP18956

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18030.830.8672empty
23030.760.8846empty
34350.720.8257empty
41760.580.8234empty
51550.550.8130empty

Interfaces

1 interface between chains.

  • A–B · 1284 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 2E0W · T391A precursor mutant protein of gamma-Glutamyltranspeptidase from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
  • P18956 · AlphaFold monomer V2.0 prediction for glutathione hydrolase proenzyme (P18956) · a predicted model of the same protein · chain A against A, TM-score 0.97

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