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- PDB-5vvn: Structure of bovine endothelial nitric oxide synthase heme domain... -

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Basic information

Entry
Database: PDB / ID: 5vvn
TitleStructure of bovine endothelial nitric oxide synthase heme domain in complex with 4-(2-(((2-Aminoquinolin-7-yl)methyl)amino)ethyl)benzonitrile
ComponentsNitric oxide synthase, endothelial
KeywordsOXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR / nitric oxide synthase / inhibitor complex / heme enzyme / OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex
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 / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / arginine catabolic process / 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 / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / arginine catabolic process / mitochondrion organization / nitric oxide biosynthetic process / caveola / FMN binding / blood coagulation / flavin adenine dinucleotide binding / NADP binding / calmodulin binding / cytoskeleton / heme binding / Golgi apparatus / metal ion binding
Similarity search - Function
Nitric-oxide synthase, eukaryote / Nitric Oxide Synthase; Chain A, domain 1 / Nitric Oxide Synthase;Heme Domain; Chain A, domain 2 / Nitric Oxide Synthase;Heme Domain;Chain A domain 2 / Nitric Oxide Synthase; Chain A, domain 1 / Nitric Oxide Synthase; Chain A, domain 3 / Bovine Endothelial Nitric Oxide Synthase Heme Domain; Chain: A,domain 3 / Nitric oxide synthase, domain 3 superfamily / Nitric oxide synthase, domain 1 superfamily / Nitric oxide synthase, domain 2 superfamily ...Nitric-oxide synthase, eukaryote / Nitric Oxide Synthase; Chain A, domain 1 / Nitric Oxide Synthase;Heme Domain; Chain A, domain 2 / Nitric Oxide Synthase;Heme Domain;Chain A domain 2 / Nitric Oxide Synthase; Chain A, domain 1 / Nitric Oxide Synthase; Chain A, domain 3 / Bovine Endothelial Nitric Oxide Synthase Heme Domain; Chain: A,domain 3 / Nitric oxide synthase, domain 3 superfamily / Nitric oxide synthase, domain 1 superfamily / Nitric oxide synthase, domain 2 superfamily / Nitric oxide synthase, N-terminal / Nitric oxide synthase (NOS) signature. / Nitric oxide synthase, N-terminal domain superfamily / Nitric oxide synthase, oxygenase domain / Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding / FAD binding domain / NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily / 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 / Ferredoxin-NADP reductase (FNR), nucleotide-binding domain / FAD-binding domain, ferredoxin reductase-type / 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 / 5,6,7,8-TETRAHYDROBIOPTERIN / Chem-P94 / PROTOPORPHYRIN IX CONTAINING FE / Nitric oxide synthase, endothelial
Similarity search - Component
Biological speciesBos taurus (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.4 Å
AuthorsLi, H. / Poulos, T.L.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM57353 United States
CitationJournal: J. Med. Chem. / Year: 2017
Title: Hydrophilic, Potent, and Selective 7-Substituted 2-Aminoquinolines as Improved Human Neuronal Nitric Oxide Synthase Inhibitors.
Authors: Pensa, A.V. / Cinelli, M.A. / Li, H. / Chreifi, G. / Mukherjee, P. / Roman, L.J. / Martasek, P. / Poulos, T.L. / Silverman, R.B.
History
DepositionMay 19, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 16, 2017Provider: repository / Type: Initial release
Revision 1.1Sep 6, 2017Group: Author supporting evidence / Database references / Category: citation / pdbx_audit_support
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _pdbx_audit_support.funding_organization
Revision 1.2Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Nitric oxide synthase, endothelial
B: Nitric oxide synthase, endothelial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)102,26015
Polymers99,4542
Non-polymers2,80613
Water1,67593
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11300 Å2
ΔGint-121 kcal/mol
Surface area32490 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.093, 106.388, 156.040
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Nitric oxide synthase, endothelial / / endothelial nitric oxide synthase / Constitutive NOS / cNOS / EC-NOS / Endothelial NOS / eNOS / NOS ...endothelial nitric oxide synthase / Constitutive NOS / cNOS / EC-NOS / Endothelial NOS / eNOS / NOS type III / NOSIII


Mass: 49727.012 Da / Num. of mol.: 2 / Fragment: UNP residues 40-482
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / Cell: endothelial / Gene: NOS3 / Plasmid: pCWori / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P29473, nitric-oxide synthase (NADPH)

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Non-polymers , 7 types, 106 molecules

#2: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#3: Chemical ChemComp-H4B / 5,6,7,8-TETRAHYDROBIOPTERIN / Tetrahydrobiopterin


Mass: 241.247 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C9H15N5O3 / Comment: neurotransmitter*YM
#4: Chemical ChemComp-P94 / 4-(2-{[(2-aminoquinolin-7-yl)methyl]amino}ethyl)benzonitrile


Mass: 302.373 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H18N4
#5: Chemical
ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H3O2
#6: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#7: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 93 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.45 Å3/Da / Density % sol: 49.8 % / Description: cube
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6
Details: 20-24% PEG3350, 0.1 M cacodylate, 140-200 mM magnesium acetate, 5 mM TCEP

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL14-1 / Wavelength: 1.087 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Apr 5, 2015 / Details: mirrors
RadiationMonochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.087 Å / Relative weight: 1
ReflectionResolution: 2.4→50 Å / Num. obs: 38722 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 5.7 % / CC1/2: 0.999 / Rmerge(I) obs: 0.076 / Rpim(I) all: 0.052 / Rsym value: 0.076 / Net I/σ(I): 16.1
Reflection shellResolution: 2.4→2.54 Å / Redundancy: 5.6 % / Rmerge(I) obs: 1.78 / Mean I/σ(I) obs: 1.1 / Num. unique obs: 3889 / CC1/2: 0.361 / Rpim(I) all: 1.257 / Rsym value: 1.78 / % possible all: 99.5

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Processing

Software
NameVersionClassification
PHENIX1.8.2_1309refinement
XDSMarch 1, 2015data reduction
Aimless0.5.8data scaling
REFMAC5.8.0049phasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: PDB entry 1NSE
Resolution: 2.4→39.232 Å / SU ML: 0.4 / Cross valid method: FREE R-VALUE / σ(F): 0.02 / Phase error: 28.71
RfactorNum. reflection% reflectionSelection details
Rfree0.2339 3668 5.02 %random
Rwork0.1798 ---
obs0.1825 38654 99.57 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.4→39.232 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6451 0 195 93 6739
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0096845
X-RAY DIFFRACTIONf_angle_d1.1519344
X-RAY DIFFRACTIONf_dihedral_angle_d15.9312460
X-RAY DIFFRACTIONf_chiral_restr0.069971
X-RAY DIFFRACTIONf_plane_restr0.0051200
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3965-2.4280.43961360.32852539X-RAY DIFFRACTION93
2.428-2.46120.43561410.31812679X-RAY DIFFRACTION100
2.4612-2.49640.37481540.32152648X-RAY DIFFRACTION100
2.4964-2.53370.39191670.30912689X-RAY DIFFRACTION100
2.5337-2.57320.31651560.2982635X-RAY DIFFRACTION100
2.5732-2.61540.35991640.3082646X-RAY DIFFRACTION100
2.6154-2.66050.40931220.28952708X-RAY DIFFRACTION100
2.6605-2.70890.32761360.27142668X-RAY DIFFRACTION100
2.7089-2.7610.29711360.27052711X-RAY DIFFRACTION100
2.761-2.81730.30881230.25392703X-RAY DIFFRACTION100
2.8173-2.87860.32911120.25092706X-RAY DIFFRACTION100
2.8786-2.94550.2781490.2322650X-RAY DIFFRACTION100
2.9455-3.01910.25381410.21772659X-RAY DIFFRACTION100
3.0191-3.10070.30681630.2142681X-RAY DIFFRACTION100
3.1007-3.19190.26481330.22662698X-RAY DIFFRACTION100
3.1919-3.29490.30871180.21912716X-RAY DIFFRACTION100
3.2949-3.41260.26941590.20572661X-RAY DIFFRACTION100
3.4126-3.54910.22411270.18192658X-RAY DIFFRACTION100
3.5491-3.71060.25361560.16582668X-RAY DIFFRACTION100
3.7106-3.9060.18351430.15482701X-RAY DIFFRACTION100
3.906-4.15050.25471170.14352706X-RAY DIFFRACTION100
4.1505-4.47050.18111620.12662635X-RAY DIFFRACTION100
4.4705-4.91970.15891180.11822712X-RAY DIFFRACTION100
4.9197-5.62980.22411200.14132674X-RAY DIFFRACTION100
5.6298-7.08610.16321610.16652661X-RAY DIFFRACTION100
7.0861-39.23680.19751540.15262620X-RAY DIFFRACTION99
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
11.2734-0.5802-0.71351.31150.50561.9181-0.0159-0.03280.0075-0.22050.1225-0.1415-0.14440.0942-0.09330.505-0.06820.00350.3612-0.02390.418411.21810.366331.807
20.6783-0.38310.61751.4732-0.93573.27250.1214-0.0695-0.05640.02880.0094-0.0168-0.0096-0.0103-0.10490.3489-0.0454-0.00240.4055-0.00720.38332.63145.73367.4967
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 67:482)
2X-RAY DIFFRACTION2(chain B and resid 69:482)

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