1D1W

BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 2-AMINOTHIAZOLINE (H4B BOUND)

Summary for 1D1W

• Entry DOI: 10.2210/pdb1d1w/pdb
• Related: 1D0C 1D0O 1D1V 1D1W 1D1X 1D1Y 1NSE
• Descriptor: NITRIC OXIDE SYNTHASE, ACETATE ION, ZINC ION, ... (9 entities in total)
• Functional Keywords: alpha-beta fold, oxidoreductase
• Biological source: Bos taurus (cattle)
• Cellular location: Cell membrane: P29473
• Total number of polymer chains: 2
• Total formula weight: 102285.95

Authors

Li, H.,Raman, C.S.,Martasek, P.,Kral, V.,Masters, B.S.S.,Poulos, T.L. (deposition date: 1999-09-21, release date: 2000-10-25, Last modification date: 2024-02-07)

Primary citation

Li, H.,Raman, C.S.,Martasek, P.,Kral, V.,Masters, B.S.,Poulos, T.L.
Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas.
J.Inorg.Biochem., 81:133-139, 2000

PubMed 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.

PubMed: 11051558
DOI: 10.1016/S0162-0134(00)00099-4

Experimental method

X-RAY DIFFRACTION (2 Å)