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Crystal structure of glutathione transferase zeta 1-1 (maleylacetoacetate isomerase) from mus musculus (form-1 crystal)

Analyse Crystal structure of glutathione transferase zeta 1-1 (maleylacetoacetate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2CZ2
Type
protein
Length
212 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Maleylacetoacetate isomerase
EC
5.2.1.2, 2.5.1.18
UniProt
Q9WVL0
Ligands
GSH
Pockets
3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMaleylacetoacetate isomerase (EC 5.2.1.2, 2.5.1.18)protein21256% helix, 8% strandQ9WVL0

Ligands and binding sites

  • GSH · Glutathione · ligand · chains A
  • GOL · Glycerol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12470.670.8436GSH
21080.430.7720empty
3510.300.7617GOL

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

  • 2CZ2 · Crystal structure of glutathione transferase zeta 1-1 (maleylacetoacetate isomerase) from… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9WVL0 · AlphaFold monomer V2.0 prediction for maleylacetoacetate isomerase (Q9WVL0) · a predicted model of the same protein · chain A against A, TM-score 0.99

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