1D1V

BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH S-ETHYL-N-PHENYL-ISOTHIOUREA (H4B BOUND)

Summary for 1D1V

Related1NSE 1D0C 1D0O 1D1V 1D1W 1D1X 1D1Y
DescriptorBOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME, ACETATE ION, ZINC ION, ... (9 entities in total)
Functional Keywordsalpha-beta fold, oxidoreductase
Biological sourceBos taurus (cattle)
Cellular locationCell membrane P29473
Total number of polymer chains2
Total molecular weight102257.99
Authors
Raman, C.S.,Li, H.,Martasek, P.,Southan, G.J.,Masters, B.S.S.,Poulos, T.L. (deposition date: 1999-09-21, release date: 2001-07-25, Last modification date: 2011-07-13)
Primary citation
Raman, C.S.,Li, H.,Martasek, P.,Babu, B.R.,Griffith, O.W.,Masters, B.S.,Poulos, T.L.
Implications for isoform-selective inhibitor design derived from the binding mode of bulky isothioureas to the heme domain of endothelial nitric-oxide synthase.
J.Biol.Chem., 276:26486-26491, 2001
PubMed: 11331290 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.M102255200
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.93 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers90.6%2.5%8.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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