1D1W: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed With 2- Aminothiazoline (h4b Bound)

Citation:
Abstract
Analyzing the active site topology and plasticity of nitric oxide synthase (NOS) and understanding enzyme-drug interactions are crucial for the development of potent, isoform-selective NOS inhibitors. A small hydrophobic pocket in the active site is identified in the bovine eNOS heme domain structures complexed with potent isothiourea inhibitors: seleno analogue of S-ethyl-isothiourea, S-isopropyl-isothiourea, and 2-aminothiazoline, respectively. These structures reveal the importance of nonpolar van der Waals contacts in addition to the well-known hydrogen bonding interactions between inhibitor and enzyme. The scaffold of a potent NOS inhibitor should be capable of donating hydrogen bonds to as well as making nonpolar contacts with amino acids in the NOS active site.
PDB ID: 1D1WDownload
MMDB ID: 14765
PDB Deposition Date: 1999/9/21
Updated in MMDB: 2000/12
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 1D1W: dimeric; determined by author and by software (PISA)
Molecular Components in 1D1W
Label Count Molecule
Proteins (2 molecules)
2
Nitric Oxide Synthase(Gene symbol: NOS3)
Molecule annotation
Chemicals (17 molecules)
1
4
2
1
3
2
4
2
5
2
6
2
7
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.