Structure of a molybdopterin-bound CNX1G domain links molybdenum and copper metabolism

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 21% strand (DSSP).

Ligands and binding sites

• 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 · chains A
• AMP · Adenosine monophosphate · ligand · chains A
• CU1 · Copper (I) ion · metal · chains A
• PPI · Propanoic acid · additive · chains A
• IMD · Imidazole · additive · chains A
• FMT · Formic acid · additive · chains A

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

Pockets

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

Compared structures

• 1UUY · Structure of a molybdopterin-bound cnx1g domain links molybdenum and copper metabolism · the same entry in another collection · chain A against A, TM-score 1.00
• Q39054 · AlphaFold monomer V2.0 prediction for molybdopterin biosynthesis protein CNX1 (Q39054) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q39054
• Elsewhere: RCSB PDB 1UUY · PDBe 1UUY · UniProt Q39054