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1FOO

BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG AND NO(H4B-FREE)

Summary for 1FOO
Entry DOI10.2210/pdb1foo/pdb
Related4NSE
DescriptorNITRIC-OXIDE SYNTHASE, CACODYLATE ION, ACETATE ION, ... (9 entities in total)
Functional Keywordsalpha-beta fold, nitric oxide synthase, oxidoreductase
Biological sourceBos taurus (cattle)
Cellular locationCell membrane: P29473
Total number of polymer chains2
Total formula weight101889.47
Authors
Raman, C.S.,Li, H.,Martasek, P.,Masters, B.S.S.,Poulos, T.L. (deposition date: 2000-08-28, release date: 2001-07-20, Last modification date: 2024-02-07)
Primary citationLi, H.,Raman, C.S.,Martasek, P.,Masters, B.S.,Poulos, T.L.
Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors.
Biochemistry, 40:5399-5406, 2001
Cited by
PubMed Abstract: The crystal structure of the endothelial nitric oxide synthase (NOS) heme domain complexed with NO reveals close hydrogen bonding interactions between NO and the terminal guanidino nitrogen of the substrate, L-arginine. Dioxygen is expected to bind in a similar mode which will facilitate proton abstraction from L-Arg to dioxygen, a required step for O-O bond cleavage. Structures of mechanism-based NOS inhibitors, N(5)-(1-iminoethyl)-L-ornithine and N-(3-(aminomethyl)benzyl)acetamidine, provide clues on how this class of compounds operate as suicide substrate inhibitors leading to heme oxidation.
PubMed: 11331003
DOI: 10.1021/bi002658v
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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