|Entry||Database: PDB / ID: 1d0o|
|Title||BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 3-BROMO-7-NITROINDAZOLE (H4B PRESENT)|
|Components||BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME|
|Keywords||OXIDOREDUCTASE / ALPHA-BETA FOLD|
|Function / homology|
Function and homology information
cellular response to laminar fluid shear stress / negative regulation of leukocyte cell-cell adhesion / nitric-oxide synthase (NADPH) / positive regulation of guanylate cyclase activity / nitric-oxide synthase activity / arginine catabolic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / mitochondrion organization / nitric oxide biosynthetic process / caveola ...cellular response to laminar fluid shear stress / negative regulation of leukocyte cell-cell adhesion / nitric-oxide synthase (NADPH) / positive regulation of guanylate cyclase activity / nitric-oxide synthase activity / arginine catabolic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / mitochondrion organization / nitric oxide biosynthetic process / caveola / FMN binding / flavin adenine dinucleotide binding / NADP binding / calmodulin binding / blood coagulation / cytoskeleton / heme binding / Golgi apparatus / metal ion binding
Similarity search - Function
Nitric-oxide synthase, eukaryote / Nitric Oxide Synthase;Heme Domain; Chain A, domain 2 / Bovine Endothelial Nitric Oxide Synthase Heme Domain; Chain: A,domain 3 / Nitric Oxide Synthase; Chain A, domain 3 / Nitric Oxide Synthase; Chain A, domain 1 / Nitric Oxide Synthase; Chain A, domain 1 / Nitric Oxide Synthase;Heme Domain;Chain A domain 2 / Nitric oxide synthase, N-terminal domain superfamily / Nitric oxide synthase, oxygenase domain / Nitric oxide synthase, N-terminal ...Nitric-oxide synthase, eukaryote / Nitric Oxide Synthase;Heme Domain; Chain A, domain 2 / Bovine Endothelial Nitric Oxide Synthase Heme Domain; Chain: A,domain 3 / Nitric Oxide Synthase; Chain A, domain 3 / Nitric Oxide Synthase; Chain A, domain 1 / Nitric Oxide Synthase; Chain A, domain 1 / Nitric Oxide Synthase;Heme Domain;Chain A domain 2 / Nitric oxide synthase, N-terminal domain superfamily / Nitric oxide synthase, oxygenase domain / Nitric oxide synthase, N-terminal / Nitric oxide synthase (NOS) signature. / NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily / Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding / FAD binding domain / Flavodoxin-like / Flavoprotein pyridine nucleotide cytochrome reductase / Flavodoxin / Oxidoreductase NAD-binding domain / Oxidoreductase FAD/NAD(P)-binding / Flavodoxin-like domain profile. / Flavodoxin/nitric oxide synthase / FAD-binding domain, ferredoxin reductase-type / Ferredoxin-NADP reductase (FNR), nucleotide-binding domain / Ferredoxin reductase-type FAD binding domain profile. / Riboflavin synthase-like beta-barrel / Flavoprotein-like superfamily / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / CACODYLIC ACID / 3-BROMO-7-NITROINDAZOLE / PROTOPORPHYRIN IX CONTAINING FE / Nitric oxide synthase, endothelial
Similarity search - Component
|Biological species||Bos taurus (cattle)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.95 Å|
|Authors||Raman, C.S. / Li, H. / Martasek, P. / Southan, G.J. / Masters, B.S.S. / Poulos, T.L.|
Journal: Biochemistry / Year: 2001
Title: Crystal structure of nitric oxide synthase bound to nitro indazole reveals a novel inactivation mechanism.
Authors: Raman, C.S. / Li, H. / Martasek, P. / Southan, G. / Masters, B.S. / Poulos, T.L.
#1: Journal: Cell(Cambridge,Mass.) / Year: 1998
Title: Crystal Structure of Constitutive Endothelial Nitric Oxide Synthase: a Paradigm for Pterin Function Involving a Novel Metal Center
Authors: Raman, C.S. / Li, H. / Martasek, P. / Kral, V. / Masters, B.S. / Poulos, T.L.
#2: Journal: Science / Year: 1998
Title: Structure of Nitric Oxide Synthase Oxygenase Dimer with Pterin and Substrate
Authors: Crane, B.R. / Arvai, A.S. / Ghosh, D.K. / Wu, C. / Getzoff, E.D. / Stuehr, D.J. / Tainer, J.A.
|Structure viewer||Molecule: |
Downloads & links
A: BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME
B: BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME
-Protein , 1 types, 2 molecules A
Mass: 49710.105 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / Cell: ENDOTHELIAL CELLS / Production host: Escherichia coli (E. coli) / References: UniProt: P29473, nitric-oxide synthase (NADPH)
-Non-polymers , 7 types, 441 molecules
|#3: Chemical|| ChemComp-ZN / ||#4: Chemical||#5: Chemical|
|#6: Chemical||#7: Chemical||#8: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.39 Å3/Da / Density % sol: 48.55 %|
|Crystal grow||Temperature: 280 K / Method: vapor diffusion, sitting drop / pH: 6.5 |
Details: PEG 4000, CACODYLATE, MAGNESIUM ACETATE, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 280K
*PLUSDetails: Raman, C.S., (1998) Cell (Cambridge,Mass.), 95, 939.
|Components of the solutions|
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1|
|Detector||Type: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 12, 1998|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1 Å / Relative weight: 1|
|Reflection||Resolution: 1.9→50 Å / Num. obs: 73044 / % possible obs: 95.7 % / Observed criterion σ(I): -3 / Redundancy: 3.2 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 8.8|
|Reflection shell||Resolution: 1.9→1.93 Å / Redundancy: 3 % / Rmerge(I) obs: 0.612 / % possible all: 93.5|
*PLUSHighest resolution: 1.95 Å / Num. measured all: 231841 / Rmerge(I) obs: 0.05
*PLUS% possible obs: 93.5 % / Mean I/σ(I) obs: 2
|Refinement||Resolution: 1.95→30 Å / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber|
Details: Residues 108 to 120 are disordered, but the tentative model was included in the refinement. Cofactor H4B was present in the protein sample used for the crystallization and have been replaced ...Details: Residues 108 to 120 are disordered, but the tentative model was included in the refinement. Cofactor H4B was present in the protein sample used for the crystallization and have been replaced by 3-Br-7-nitro-indazole during the crystal growth.
|Refinement step||Cycle: LAST / Resolution: 1.95→30 Å|
|Refine LS restraints|
|LS refinement shell||Resolution: 1.95→2.04 Å / Total num. of bins used: 8 |
*PLUSName: X-PLOR / Version: 3.851 / Classification: refinement
*PLUSLowest resolution: 30 Å / σ(F): 2 / % reflection Rfree: 5 % / Rfactor obs: 0.2 / Rfactor Rwork: 0.2
|Refine LS restraints|
|LS refinement shell|
*PLUSRfactor Rfree: 0.313 / % reflection Rfree: 3.4 % / Rfactor Rwork: 0.303
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