Structure of bovine endothelial nitric oxide synthase heme domain in complex with (9aS)-2-amino-9a-methyl-6,7,8,9,9a,10-hexahydrobenzo[g]pteridin-4(3H)-one
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 synthase activity / nitric oxide mediated signal transduction / arginine catabolic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / mitochondrion organization / 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 synthase activity / nitric oxide mediated signal transduction / arginine catabolic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / mitochondrion organization / negative regulation of blood pressure / nitric oxide biosynthetic process / response to hormone / caveola / blood coagulation / FMN binding / flavin adenine dinucleotide binding / NADP binding / response to lipopolysaccharide / cytoskeleton / calmodulin binding / heme binding / Golgi apparatus / metal ion binding / nucleus / 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: 2.33→50 Å / Num. obs: 42159 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 4.4 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 22.03
Reflection shell
Resolution: 2.33→2.41 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.86 / Mean I/σ(I) obs: 2.13 / % possible all: 97.9
-
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: 2.33→88.04 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.942 / SU B: 13.626 / SU ML: 0.169 / Cross valid method: THROUGHOUT / ESU R: 0.295 / ESU R Free: 0.223 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS 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
0.22703
2102
5 %
RANDOM
Rwork
0.16951
-
-
-
obs
0.17233
40040
99.58 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK