Human aldehyde oxidase SNP R1231H in complex with raloxifene

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

Ligands and binding sites

• FES · Fe2/s2 (inorganic) cluster · ligand · 4 copies · chains A, B
• RAL · Raloxifene · ligand · 4 copies · chains A, B
• MTE · Phosphonic acidmono-(2-amino-5,6-dimercapto-4-oxo-3,7,8A,9,10,10A-hexahydro-4H-8-oxa-1,3,9,10-tetraaza-anthracen-7-ylmethyl)ester · ligand · 2 copies · chains A, B
• MOS · Dioxothiomolybdenum(vi) ion · ligand · 2 copies · chains A, B
• FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
• GOL · Glycerol · additive · 3 copies · chains A, B
• MLI · Malonate ion · additive · 2 copies · chains A, B
• PG6 · 1-(2-methoxy-ethoxy)-2-{2-[2-(2-methoxy-ethoxy]-ethoxy}-ethane · additive · chains A, B
• DMS · Dimethyl sulfoxide · additive · chains B

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 2713 Ų buried · 67 hydrogen bonds · protein-protein

Compared structures

• 7OPN · Human Aldehyde Oxidase SNP R1231H in complex with Raloxifene · the same entry in another collection · chain A against A, TM-score 1.00
• Q06278 · AlphaFold monomer V2.0 prediction for aldehyde oxidase (Q06278) · a predicted model of the same protein · chain B against A, TM-score 1.00

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 Q06278
• Elsewhere: RCSB PDB 7OPN · PDBe 7OPN · UniProt Q06278