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- PDB-1zvl: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain complexed wit... -

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Basic information

Entry
Database: PDB / ID: 1zvl
TitleRat Neuronal Nitric Oxide Synthase Oxygenase Domain complexed with natural substrate L-Arg.
ComponentsNitric-oxide synthase, brainNitric oxide synthase
KeywordsOXIDOREDUCTASE / RAT NNOSOXY / Targeting Tetrahydrobiopterin Binding Site.
Function / homology
Function and homology information


synaptic signaling by nitric oxide / Nitric oxide stimulates guanylate cyclase / positive regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process / negative regulation of hepatic stellate cell contraction / negative regulation of vasoconstriction / ROS and RNS production in phagocytes / negative regulation of iron ion transmembrane transport / Ion homeostasis / azurophil granule / retrograde trans-synaptic signaling by nitric oxide ...synaptic signaling by nitric oxide / Nitric oxide stimulates guanylate cyclase / positive regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process / negative regulation of hepatic stellate cell contraction / negative regulation of vasoconstriction / ROS and RNS production in phagocytes / negative regulation of iron ion transmembrane transport / Ion homeostasis / azurophil granule / retrograde trans-synaptic signaling by nitric oxide / negative regulation of cytosolic calcium ion concentration / response to nitric oxide / positive regulation of sodium ion transmembrane transport / postsynaptic specialization, intracellular component / positive regulation of the force of heart contraction / negative regulation of potassium ion transport / cadmium ion binding / regulation of heart contraction / negative regulation of serotonin uptake / multicellular organismal response to stress / regulation of sodium ion transport / calyx of Held / behavioral response to cocaine / sodium channel regulator activity / striated muscle contraction / peptidyl-cysteine S-nitrosylation / postsynaptic density, intracellular component / negative regulation of calcium ion transport / regulation of neurogenesis / negative regulation of hydrolase activity / negative regulation of insulin secretion / response to vitamin E / xenobiotic catabolic process => GO:0042178 / negative regulation of heart contraction / regulation of sensory perception of pain / nitric-oxide synthase (NADPH) / positive regulation of guanylate cyclase activity / negative regulation of blood pressure / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen / T-tubule / nitric oxide mediated signal transduction / sarcoplasmic reticulum membrane / cellular response to epinephrine stimulus / vesicle membrane / negative regulation of peptidyl-serine phosphorylation / nitric-oxide synthase activity / NADPH binding / arginine catabolic process / response to organonitrogen compound / positive regulation of histone acetylation / response to hormone / sarcoplasmic reticulum / nitric oxide biosynthetic process / response to nicotine / response to peptide hormone / muscle contraction / response to activity / cell periphery / response to nutrient levels / secretory granule / positive regulation of long-term synaptic potentiation / photoreceptor inner segment / sarcolemma / response to organic cyclic compound / response to lead ion / cellular response to growth factor stimulus / Z disc / phosphoprotein binding / female pregnancy / establishment of protein localization / vasodilation / calcium-dependent protein binding / positive regulation of neuron death / cellular response to mechanical stimulus / FMN binding / brain development / scaffold protein binding / flavin adenine dinucleotide binding / response to heat / NADP binding / transmembrane transporter binding / nuclear membrane / positive regulation of peptidyl-serine phosphorylation / response to lipopolysaccharide / ATPase binding / response to estrogen / response to ethanol / mitochondrial outer membrane / negative regulation of neuron apoptotic process / calmodulin binding / dendritic spine / postsynaptic density / response to hypoxia / aging / cytoskeleton / oxidoreductase activity / negative regulation of cell population proliferation / glutamatergic synapse / synapse / membrane raft
Similarity search - Function
Nitric-oxide synthase, eukaryote / 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 1 / Nitric Oxide Synthase; Chain A, domain 3 / Bovine Endothelial Nitric Oxide Synthase Heme Domain; Chain: A,domain 3 / Nitric oxide synthase, N-terminal / Nitric oxide synthase, N-terminal domain superfamily / Nitric oxide synthase (NOS) signature. ...Nitric-oxide synthase, eukaryote / 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 1 / Nitric Oxide Synthase; Chain A, domain 3 / Bovine Endothelial Nitric Oxide Synthase Heme Domain; Chain: A,domain 3 / Nitric oxide synthase, N-terminal / Nitric oxide synthase, N-terminal domain superfamily / Nitric oxide synthase (NOS) signature. / Nitric oxide synthase, oxygenase domain / Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding / NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily / FAD binding domain / Flavodoxin-like / Flavoprotein pyridine nucleotide cytochrome reductase / Flavodoxin / Oxidoreductase FAD/NAD(P)-binding / Oxidoreductase NAD-binding domain / Flavodoxin-like domain profile. / Flavodoxin/nitric oxide synthase / FAD-binding domain, ferredoxin reductase-type / Ferredoxin reductase-type FAD binding domain profile. / Ferredoxin-NADP reductase (FNR), nucleotide-binding domain / Riboflavin synthase-like beta-barrel / PDZ domain / Flavoprotein-like superfamily / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
ARGININE / 5,6,7,8-TETRAHYDROBIOPTERIN / PROTOPORPHYRIN IX CONTAINING FE / Nitric oxide synthase, brain
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsMatter, H. / Kumar, H.S. / Fedorov, R. / Frey, A. / Kotsonis, P. / Hartmann, E. / Frohlich, L.G. / Reif, A. / Pfleiderer, W. / Scheurer, P. ...Matter, H. / Kumar, H.S. / Fedorov, R. / Frey, A. / Kotsonis, P. / Hartmann, E. / Frohlich, L.G. / Reif, A. / Pfleiderer, W. / Scheurer, P. / Ghosh, D.K. / Schlichting, I. / Schmidt, H.H.
CitationJournal: J.Med.Chem. / Year: 2005
Title: Structural Analysis of Isoform-Specific Inhibitors Targeting the Tetrahydrobiopterin Binding Site of Human Nitric Oxide Synthases.
Authors: Matter, H. / Kumar, H.S. / Fedorov, R. / Frey, A. / Kotsonis, P. / Hartmann, E. / Frohlich, L.G. / Reif, A. / Pfleiderer, W. / Scheurer, P. / Ghosh, D.K. / Schlichting, I. / Schmidt, H.H.
History
DepositionJun 2, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 2, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 11, 2017Group: Refinement description / Category: software

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Nitric-oxide synthase, brain
B: Nitric-oxide synthase, brain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)99,2929
Polymers97,1602
Non-polymers2,1317
Water5,837324
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8910 Å2
ΔGint-77 kcal/mol
Surface area34670 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)52.360, 111.289, 165.184
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
DetailsThe biological assembly is represented by chains A and B in asymmetric unit.

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Nitric-oxide synthase, brain / Nitric oxide synthase / NOS / type I / Neuronal NOS / N-NOS / nNOS / Constitutive NOS / NC-NOS / BNOS


Mass: 48580.203 Da / Num. of mol.: 2 / Fragment: NEURONAL OXIDE SYNTHASE OXYGENASE DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Nos1, Bnos / Plasmid: PCWORI / Production host: Escherichia coli (E. coli) / References: UniProt: P29476, nitric-oxide synthase (NADPH)

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Non-polymers , 5 types, 331 molecules

#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#4: 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
#5: Chemical ChemComp-ARG / ARGININE / Arginine


Type: L-peptide linking / Mass: 175.209 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H15N4O2
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 324 / 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: 2.604 Å3/Da / Density % sol: 50.95 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: HEPES, DTT, PEG3350, EPPS, NACL, GLYCEROL, H4B, beta-MERCAPTOETHANOL., pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: May 2, 2002
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.933 Å / Relative weight: 1
ReflectionResolution: 2.5→20 Å / Num. all: 34267 / Num. obs: 32016 / % possible obs: 93.4 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 5.7 % / Biso Wilson estimate: 38.67 Å2 / Rsym value: 0.092 / Net I/σ(I): 14.3
Reflection shellResolution: 2.5→2.6 Å / Mean I/σ(I) obs: 4.5 / Rsym value: 0.344 / % possible all: 79.6

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Processing

Software
NameVersionClassification
ProDCdata collection
XDSdata reduction
AMoREphasing
CNS1refinement
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.5→8 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.249 1600 RANDOM
Rwork0.201 --
all0.203 32016 -
obs0.203 32016 -
Refinement stepCycle: LAST / Resolution: 2.5→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6836 0 145 324 7305

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