Structure of bovine endothelial nitric oxide synthase heme domain in complex with (9aS)-2-amino-9a-methyl-8,9,9a,10-tetrahydrobenzo[g]pteridine-4,6(3H,7H)-dione
Components
NITRIC OXIDE SYNTHASE, ENDOTHELIAL
Keywords
OXIDOREDUCTASE / COFACTOR ANALOG COMPLEX
Function / homology
Function and homology information
cellular response to laminar fluid shear stress / positive regulation of guanylate cyclase activity / negative regulation of leukocyte cell-cell adhesion / nitric-oxide synthase (NADPH) / nitric oxide mediated signal transduction / nitric-oxide synthase activity / arginine catabolic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / nitric oxide biosynthetic process / negative regulation of blood pressure ...cellular response to laminar fluid shear stress / positive regulation of guanylate cyclase activity / negative regulation of leukocyte cell-cell adhesion / nitric-oxide synthase (NADPH) / nitric oxide mediated signal transduction / nitric-oxide synthase activity / arginine catabolic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / nitric oxide biosynthetic process / negative regulation of blood pressure / response to hormone / mitochondrion organization / caveola / blood coagulation / FMN binding / NADP binding / flavin adenine dinucleotide binding / response to lipopolysaccharide / cytoskeleton / calmodulin binding / heme binding / Golgi apparatus / nucleus / metal ion binding / plasma membrane / cytosol Similarity search - Function
NITRICOXIDESYNTHASE, ENDOTHELIAL / CONSTITUTIVE NOS / CNOS / EC-NOS / ENDOTHELIAL NOS / ENOS / NOS TYPE III / NOSIII / ENDOTHELIAL ...CONSTITUTIVE NOS / CNOS / EC-NOS / ENDOTHELIAL NOS / ENOS / NOS TYPE III / NOSIII / ENDOTHELIAL NITRIC OXIDE SYNTHASE
Mass: 49727.012 Da / Num. of mol.: 2 / Fragment: HEME DOMAIN, RESIDUES 40-482 Source method: isolated from a genetically manipulated source Source: (gene. exp.) BOS TAURUS (cattle) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P29473, nitric-oxide synthase (NADPH)
Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.12709 Å / Relative weight: 1
Reflection
Resolution: 2.48→50 Å / Num. obs: 35505 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 3.9 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 22.85
Reflection shell
Resolution: 2.48→2.57 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.69 / Mean I/σ(I) obs: 2.01 / % possible all: 99.6
-
Processing
Software
Name
Version
Classification
REFMAC
5.6.0117
refinement
HKL-2000
datareduction
SCALEPACK
datascaling
REFMAC
phasing
Refinement
Method to determine structure: OTHER Starting model: NONE Resolution: 2.48→87.9 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.938 / SU B: 23.395 / SU ML: 0.245 / Cross valid method: THROUGHOUT / ESU R: 0.452 / ESU R Free: 0.272 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED. RESIDUES 110 TO 120 IN CHAIN A AND 112-120 IN CHAIN B ARE DISORDERED.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.24223
1762
5 %
RANDOM
Rwork
0.18367
-
-
-
obs
0.18654
33702
99.43 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK