Structure of human endothelial nitric oxide synthase heme domain in complex with 7-(3-(2-AMINOETHYL)PHENYL)-4-methylquinolin-2-amine

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 15% strand (DSSP).

Ligands and binding sites

• HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
• H4B · 5,6,7,8-tetrahydrobiopterin · ligand · 4 copies · chains A, B, C, D
• OUG · 7-[3-(aminomethyl)phenyl]-4-methylquinolin-2-amine · ligand · 4 copies · chains A, B, C, D
• GD · Gadolinium atom · metal · 4 copies · chains A, B, C, D
• ZN · Zinc ion · metal · 2 copies · chains A, B, C, D
• BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · 14 copies · chains A, D, C, B
• ACT · Acetate ion · additive · 4 copies · chains A, B, C, D
• GOL · Glycerol · additive · 2 copies · chains A, C

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

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Interfaces

4 interfaces between chains.

• A–B · 2820 Ų buried · 41 hydrogen bonds · protein-protein
• C–D · 2753 Ų buried · 39 hydrogen bonds · protein-protein
• A–D · 508 Ų buried · 4 hydrogen bonds · protein-protein
• A–C · 59 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

• 6POV · Structure of human endothelial nitric oxide synthase heme domain in complex with… · the same entry in another collection · 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 P29474
• Elsewhere: RCSB PDB 6POV · PDBe 6POV · UniProt P29474