Crystal structure of human phenylethanolamine N-methyltransferase (PNMT) in complex with (2S)-2-amino-4-((((2R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl)(3-(7,8-dichloro-1,2,3,4-tetrahydroisoquinolin-4-yl)propyl)amino)butanoic acid and AdoHcy (SAH)

Structure

x-ray diffraction · resolution 2.76 · 2 distinct chains · 37% helix, 25% strand (DSSP).

Ligands and binding sites

• SAH · S-adenosyl-L-homocysteine · ligand · chains A
• U87 · 5'-([(3S)-3-amino-3-carboxypropyl]{3-[(4R)-7,8-dichloro-1,2,3,4-tetrahydroisoquinolin-4-yl]propyl}amino)-5'-deoxyadenosine · ligand · chains B
• CD · Cadmium ion · metal · chains A
• K · Potassium ion · metal · chains A
• EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 545 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

• 6WS1 · Crystal structure of human phenylethanolamine N-methyltransferase (pnmt) in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
• P11086 · AlphaFold monomer V2.0 prediction for phenylethanolamine N-methyltransferase (P11086) · 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 P11086
• Elsewhere: RCSB PDB 6WS1 · PDBe 6WS1 · UniProt P11086