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- PDB-4jsi: Structure of rat neuronal nitric oxide synthase heme domain in co... -

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Basic information

Entry
Database: PDB / ID: 4jsi
TitleStructure of rat neuronal nitric oxide synthase heme domain in complex with 6-((3-(((3-fluorophenethyl)amino)methyl)phenoxy)methyl)-4-methylpyridin-2-amine
ComponentsNitric oxide synthase, brain
KeywordsOXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR / nitric oxide synthase / OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex
Function / homology
Function and homology information


Nitric oxide stimulates guanylate cyclase / synaptic signaling by nitric oxide / 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 ...Nitric oxide stimulates guanylate cyclase / synaptic signaling by nitric oxide / 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 / striated muscle contraction / sodium channel regulator activity / 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 / cell periphery / response to activity / 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; 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 3 / Nitric Oxide Synthase; Chain A, domain 1 / Bovine Endothelial Nitric Oxide Synthase Heme Domain; Chain: A,domain 3 / Nitric oxide synthase, N-terminal domain superfamily / Nitric oxide synthase, N-terminal / Nitric oxide synthase, oxygenase domain ...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 3 / Nitric Oxide Synthase; Chain A, domain 1 / Bovine Endothelial Nitric Oxide Synthase Heme Domain; Chain: A,domain 3 / Nitric oxide synthase, N-terminal domain superfamily / Nitric oxide synthase, N-terminal / Nitric oxide synthase, oxygenase domain / Nitric oxide synthase (NOS) signature. / FAD binding domain / Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding / NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily / 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 / Ferredoxin reductase-type FAD binding domain profile. / FAD-binding domain, ferredoxin reductase-type / 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
ACETATE ION / 5,6,7,8-TETRAHYDROBIOPTERIN / Chem-Q05 / PROTOPORPHYRIN IX CONTAINING FE / Nitric oxide synthase, brain
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.09 Å
AuthorsLi, H. / Poulos, T.L.
CitationJournal: Bioorg.Med.Chem. / Year: 2013
Title: In search of potent and selective inhibitors of neuronal nitric oxide synthase with more simple structures.
Authors: Jing, Q. / Li, H. / Fang, J. / Roman, L.J. / Martasek, P. / Poulos, T.L. / Silverman, R.B.
History
DepositionMar 22, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 7, 2013Provider: repository / Type: Initial release
Revision 1.1Aug 21, 2013Group: Database references
Revision 1.2Nov 15, 2017Group: Refinement description / Category: software / Item: _software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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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)100,25511
Polymers97,6252
Non-polymers2,6309
Water3,999222
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9810 Å2
ΔGint-85 kcal/mol
Surface area32880 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)51.597, 110.778, 164.565
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, brain / / BNOS / Constitutive NOS / NC-NOS / NOS type I / Neuronal NOS / N-NOS / nNOS / Peptidyl-cysteine S- ...BNOS / Constitutive NOS / NC-NOS / NOS type I / Neuronal NOS / N-NOS / nNOS / Peptidyl-cysteine S-nitrosylase NOS1


Mass: 48812.527 Da / Num. of mol.: 2 / Fragment: heme domain (UNP residues 297-718)
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) / Strain (production host): BL21(DE3) / References: UniProt: P29476, nitric-oxide synthase (NADPH)

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Non-polymers , 6 types, 231 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-Q05 / 6-{[3-({[2-(3-fluorophenyl)ethyl]amino}methyl)phenoxy]methyl}-4-methylpyridin-2-amine


Mass: 365.444 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C22H24FN3O
#5: Chemical ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#6: Chemical ChemComp-ZN / ZINC ION


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


Mass: 18.015 Da / Num. of mol.: 222 / 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: 2.41 Å3/Da / Density % sol: 48.94 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5.8
Details: 20-24% PEG3350, 0.1 M MES, 100 mM ammonium acetate, 10% ethylene glycol, 5 mM GSH, 30 uM SDS, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.097 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 19, 2010 / Details: mirrors
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.097 Å / Relative weight: 1
ReflectionResolution: 2.09→50 Å / Num. obs: 56724 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 4 % / Biso Wilson estimate: 33.3 Å2 / Rmerge(I) obs: 0.075 / Rsym value: 0.075 / Net I/σ(I): 22.6
Reflection shellResolution: 2.09→2.13 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.656 / Mean I/σ(I) obs: 2.3 / Rsym value: 0.656 / % possible all: 99.9

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Processing

Software
NameVersionClassification
Blu-IceIcedata collection
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling
REFMACphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: PDB ENTRY 1OM4
Resolution: 2.09→40.7 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.939 / SU B: 13.809 / SU ML: 0.167 / Cross valid method: THROUGHOUT / ESU R: 0.217 / ESU R Free: 0.187 / Stereochemistry target values: Engh & Huber / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.24139 2786 4.9 %RANDOM
Rwork0.19323 ---
obs0.19563 53714 99.01 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 50.306 Å2
Baniso -1Baniso -2Baniso -3
1-7 Å2-0 Å2-0 Å2
2---1.09 Å20 Å2
3----5.91 Å2
Refinement stepCycle: LAST / Resolution: 2.09→40.7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6658 0 183 222 7063
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0197056
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.5641.9729602
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.2525818
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.03623.855332
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.234151169
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.3471541
X-RAY DIFFRACTIONr_chiral_restr0.1110.2994
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.0215431
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.09→2.141 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.388 163 -
Rwork0.324 3898 -
obs-3898 97.78 %
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)
10.11740.0005-0.34310.1337-0.16232.9315-0.03020.0545-0.01430.0271-0.0538-0.0298-0.0922-0.19150.08390.03130.0013-0.0030.2203-0.01010.166911.2394.85922.62
20.1914-0.07-0.19860.37370.19521.2698-0.0017-0.05990.0286-0.049-0.0310.01290.01520.01760.03270.00910.01890.00660.20820.00210.20312.0314.86359.992
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A299 - 716
2X-RAY DIFFRACTION1A801 - 804
3X-RAY DIFFRACTION2B299 - 718
4X-RAY DIFFRACTION2B801 - 804

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