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Gamma-glutamyltranspeptidase from pseudomonas nitroreducens complexed with L-don

Analyse Gamma-glutamyltranspeptidase from pseudomonas nitroreducens complexed with L-don in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7D9E
Type
protein
Length
530 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gamma-glutamyltransferase 1 threonine peptidase. merops family T03
UniProt
A0A239KXH0
Ligands
DON
Pockets
2 · best druggability 0.65

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AGamma-glutamyltransferase 1 threonine peptidase. merops family T03protein33750% helix, 12% strandA0A239KXH0
BGamma-glutamyltransferase 1 threonine peptidase. merops family T03protein19319% helix, 30% strandA0A239KXH0

Ligands and binding sites

  • DON · 6-diazenyl-5-oxo-L-norleucine · ligand · chains A, B
  • GOL · Glycerol · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12420.650.8333empty
2610.410.8016empty

Interfaces

1 interface between chains.

  • A–B · 5870 Ų buried · 108 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 7D9E · Gamma-glutamyltranspeptidase from Pseudomonas nitroreducens complexed with L-DON · the same entry in another collection · chain A against A, TM-score 1.00

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