› 7us7

X-ray diffraction
1.93Å resolution

Structure of human neuronal nitric oxide synthase R354A/G357D mutant heme domain in complex with 6-(4-(dimethylamino)but-1-yn-1-yl)-4-methylpyridin-2-amine

Released:
DOI: 10.2210/pdb7us7/pdb
PDB entry 7us7 coloured by chain, front view.
PDB entry 7us7 coloured by chain, side view.
PDB entry 7us7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
2-Aminopyridines with a shortened amino sidechain as potent, selective, and highly permeable human neuronal nitric oxide synthase inhibitors.
Vasu D, Li H, Hardy CD, Poulos TL, Silverman RB
Bioorg Med Chem 69 116878 (2022)
PMID: 35772285

Function and Biology Details

Reaction catalysed: 
(1a) 2 L-arginine + 2 NADPH + 2 O(2) = 2 N(omega)-hydroxy-L-arginine + 2 NADP(+) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151514 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitric oxide synthase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 423 amino acids
Theoretical weight: 49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli #1/H766
UniProt:
  • Canonical: P29475 (Residues: 302-722; Coverage: 29%)
Gene name: NOS1
Sequence domains: Nitric oxide synthase, oxygenase domain

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
4 bound ligands:
Ligand H4B 4 x H4B
Ligand O5X 4 x O5X
Ligand GOL 7 x GOL
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P21
Unit cell:
a: 52.377Å b: 117.775Å c: 165.297Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.175 0.214
Expression system: Escherichia coli #1/H766

Quick links

Citations

1 review citation

Neuronal Nitric Oxide Synthase and Post-Translational Modifications in the Development of Central Nervous System Diseases: Implications and Regulation.
Maccallini et al. (2023)
2 other articles