X-ray crystal structure of human heme oxygenase-1 with (2R, 4S)-2-[2-(4-CHLOROPHENYL)ETHYL]-2-[(1H-imidazol-1-yl) methyl]-4[((5-trifluoromethylpyridin-2-YL)THIO)METHYL]-1,3- dioxolane: a novel, inducible binding mode

Structure

x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).

Ligands and binding sites

• HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
• Q80 · 2-({[(2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-(1H-imidazol-1-ylmethyl)-1,3-dioxolan-4-yl]methyl}sulfanyl)-5-(trifluoromethyl)pyridine · ligand · chains B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 1171 Ų buried · 21 hydrogen bonds · protein-protein

Compared structures

• 3HOK · X-ray Crystal Structure of Human Heme Oxygenase-1 with (2R… · the same entry in another collection · chain A against A, TM-score 1.00
• P09601 · AlphaFold monomer V2.0 prediction for heme oxygenase 1 (P09601) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P09601
• Elsewhere: RCSB PDB 3HOK · PDBe 3HOK · UniProt P09601