2-hydroxychromene-2-carboxylate isomerase: a kappa class glutathione- S-transferase from pseudomonas putida

Structure

x-ray diffraction · 1 distinct chain · 61% helix, 10% strand (DSSP).

Ligands and binding sites

• GSH · Glutathione · ligand · chains A
• TOH · (3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoic acid · ligand · chains A
• 2C2 · (2S)-2-hydroxy-2H-chromene-2-carboxylic acid · ligand · chains A
• PO4 · Phosphate ion · ion · 3 copies · chains A
• CXS · 3-cyclohexyl-1-propylsulfonic acid · additive · chains A

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.

Modifications

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

Compared structures

• 2IME · 2-Hydroxychromene-2-carboxylate Isomerase: a Kappa Class Glutathione-S-Transferase from… · the same entry in another collection · chain A against A, TM-score 1.00
• Q51948 · AlphaFold monomer V2.0 prediction for 2-hydroxychromene-2-carboxylate isomerase (Q51948) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q51948
• Elsewhere: RCSB PDB 2IME · PDBe 2IME · UniProt Q51948