Crystal structure of human xanthine oxidoreductase mutant, GLU803VAL

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 23% strand (DSSP).

Ligands and binding sites

• FES · Fe2/s2 (inorganic) cluster · ligand · 8 copies · chains A, B, C, D
• BCT · Bicarbonate ion · ligand · 4 copies · chains A, B, C, D
• FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
• 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 · 4 copies · chains A, B, C, D
• MOM · Hydroxy(dioxo)molybdenum · ligand · 4 copies · chains A, B, C, D
• SAL · 2-hydroxybenzoic acid · ligand · 4 copies · chains A, B, C, D
• CA · Calcium ion · metal · 8 copies · chains A, B, C, D

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

3 interfaces between chains.

• A–B · 2777 Ų buried · 44 hydrogen bonds · protein-protein
• C–D · 2730 Ų buried · 43 hydrogen bonds · protein-protein
• A–C · 244 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

• 2E1Q · Crystal Structure of Human Xanthine Oxidoreductase mutant, Glu803Val · the same entry in another collection · chain A against A, TM-score 1.00
• P47989 · AlphaFold monomer V2.0 prediction for xanthine DEHYDROGENASE/OXIDASE (P47989) · a predicted model of the same protein · chain A 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 P47989
• Elsewhere: RCSB PDB 2E1Q · PDBe 2E1Q · UniProt P47989