Pavine N-methyltransferase in complex with tetrahydropapaverine and S- adenosylhomocysteine pH 7.25

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 18% strand (DSSP).

Ligands and binding sites

• SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
• S9T · (1~{S})-1-[(3,4-dimethoxyphenyl)methyl]-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline · ligand · 2 copies · chains A, B
• R9T · (1~{R})-1-[(3,4-dimethoxyphenyl)methyl]-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline · ligand · 2 copies · chains A, 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 · 1097 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

• 5KOK · Pavine N-methyltransferase in complex with Tetrahydropapaverine and… · the same entry in another collection · chain A against A, TM-score 1.00
• C3SBW0 · AlphaFold monomer V2.0 prediction for pavine N-methyltransferase (C3SBW0) · a predicted model of the same protein · chain B 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 C3SBW0
• Elsewhere: RCSB PDB 5KOK · PDBe 5KOK · UniProt C3SBW0