Structure of bovine endothelial nitric oxide synthase heme domain (H4B-free) supplemented with 50uM Zn acetate and with poor binding of 6-acetyl-2-amino-7,7-dimethyl-7,8-dihydropteridin-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 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 / mitochondrion organization / response to hormone / 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
Mass: 18.015 Da / Num. of mol.: 231 / Source method: isolated from a natural source / Formula: H2O
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Details
Nonpolymer details
CACODYLIC ACID (CAD): THIS DIMETHYL ARSENIC MOIETY IS CONSIDERED BOUND TO CYSTEINE 384 TO FORM S- ...CACODYLIC ACID (CAD): THIS DIMETHYL ARSENIC MOIETY IS CONSIDERED BOUND TO CYSTEINE 384 TO FORM S-DIMETHYLARSENYL-L-CYSTEINE
Sequence details
RESIDUE 100 IS FOUND AS AN ARG IN STRUCTURE BUT IS A CYS IN DATABASE
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.5 Å3/Da / Density % sol: 50.7 % / Description: NONE
Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: May 27, 2012 / Details: MIRRORS
Radiation
Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.97946 Å / Relative weight: 1
Reflection
Resolution: 2.31→50 Å / Num. obs: 42009 / % possible obs: 97.9 % / Observed criterion σ(I): -3 / Redundancy: 4 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 24.04
Reflection shell
Resolution: 2.31→2.39 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.69 / Mean I/σ(I) obs: 2.07 / % possible all: 90
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Processing
Software
Name
Version
Classification
REFMAC
5.8.0049
refinement
HKL-2000
datareduction
SCALEPACK
datascaling
REFMAC
phasing
Refinement
Method to determine structure: OTHER Starting model: NONE Resolution: 2.31→50 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.949 / SU B: 13.619 / SU ML: 0.163 / Cross valid method: THROUGHOUT / ESU R: 0.266 / ESU R Free: 0.208 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS. RESIDUES 108 TO 120 IN CHAIN A AND 109-120 IN CHAIN B ARE DISORDERED.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.21358
2094
5 %
RANDOM
Rwork
0.15479
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obs
0.15769
39877
98.11 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK