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- PDB-1m9t: Inducible Nitric Oxide Synthase with 3-Bromo-7-Nitroindazole bound -

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Basic information

Entry
Database: PDB / ID: 1m9t
TitleInducible Nitric Oxide Synthase with 3-Bromo-7-Nitroindazole bound
Componentsinducible nitric oxide synthaseNitric oxide synthase
KeywordsOXIDOREDUCTASE
Function / homology
Function and homology information


Nitric oxide stimulates guanylate cyclase / ROS and RNS production in phagocytes / G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger / Peroxisomal protein import / cAMP-dependent protein kinase regulator activity / prostaglandin secretion / positive regulation of killing of cells of another organism / tetrahydrobiopterin binding / arginine binding / cortical cytoskeleton ...Nitric oxide stimulates guanylate cyclase / ROS and RNS production in phagocytes / G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger / Peroxisomal protein import / cAMP-dependent protein kinase regulator activity / prostaglandin secretion / positive regulation of killing of cells of another organism / tetrahydrobiopterin binding / arginine binding / cortical cytoskeleton / superoxide metabolic process / cellular response to cytokine stimulus / cGMP-mediated signaling / regulation of cytokine production involved in inflammatory response / nitric-oxide synthase binding / regulation of insulin secretion / peptidyl-cysteine S-nitrosylation / blood vessel remodeling / regulation of heart contraction / response to tumor necrosis factor / nitric-oxide synthase (NADPH) / positive regulation of guanylate cyclase activity / nitric oxide mediated signal transduction / vesicle membrane / cellular response to organic cyclic compound / nitric-oxide synthase activity / arginine catabolic process / negative regulation of blood pressure / response to hormone / nitric oxide biosynthetic process / cellular response to type II interferon / response to bacterium / Hsp90 protein binding / positive regulation of interleukin-8 production / positive regulation of interleukin-6 production / peroxisome / circadian rhythm / negative regulation of protein catabolic process / regulation of blood pressure / beta-catenin binding / cellular response to xenobiotic stimulus / FMN binding / actin binding / regulation of cell population proliferation / flavin adenine dinucleotide binding / NADP binding / response to lipopolysaccharide / calmodulin binding / response to hypoxia / cellular response to lipopolysaccharide / cadherin binding / intracellular signal transduction / inflammatory response / oxidoreductase activity / positive regulation of apoptotic process / defense response to bacterium / negative regulation of gene expression / heme binding / protein kinase binding / perinuclear region of cytoplasm / signal transduction / protein homodimerization activity / extracellular space / metal ion binding / identical protein binding / plasma membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
Nitric Oxide Synthase; Chain A, domain 3 / Bovine Endothelial Nitric Oxide Synthase Heme Domain; Chain: A,domain 3 / 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, eukaryote / Nitric oxide synthase, domain 1 superfamily / Nitric oxide synthase, domain 2 superfamily / Nitric oxide synthase, domain 3 superfamily ...Nitric Oxide Synthase; Chain A, domain 3 / Bovine Endothelial Nitric Oxide Synthase Heme Domain; Chain: A,domain 3 / 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, eukaryote / Nitric oxide synthase, domain 1 superfamily / Nitric oxide synthase, domain 2 superfamily / Nitric oxide synthase, domain 3 superfamily / Nitric oxide synthase, N-terminal domain superfamily / Nitric oxide synthase, oxygenase domain / Nitric oxide synthase, N-terminal / Nitric oxide synthase (NOS) signature. / FAD binding domain / NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily / Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding / 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-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
5,6,7,8-TETRAHYDROBIOPTERIN / PROTOPORPHYRIN IX CONTAINING FE / 3-BROMO-7-NITROINDAZOLE / Nitric oxide synthase, inducible
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsRosenfeld, R.J. / Garcin, E.D. / Panda, K. / Andersson, G. / Aberg, A. / Wallace, A.V. / Stuehr, D.J. / Tainer, J.A. / Getzoff, E.D.
Citation
Journal: Biochemistry / Year: 2002
Title: Conformational Changes in Nitric Oxide Synthases Induced by Chlorzoxazone and Nitroindazoles: Crystallographic and Computational Analyses of Inhibitor Potency
Authors: Rosenfeld, R.J. / Garcin, E.D. / Panda, K. / Andersson, G. / Aberg, A. / Wallace, A.V. / Morris, G.M. / Olson, A.J. / Stuehr, D.J. / Tainer, J.A. / Getzoff, E.D.
#1: Journal: Science / Year: 1998
Title: Structure of nitric oxide synthase oxygenase dimer with pterin and substrate
Authors: Crane, B.R. / Arvai, A.S. / Ghosh, D.K. / Wu, C. / Getzoff, E.D. / Stuehr, D.J. / Tainer, J.A.
History
DepositionSep 5, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 11, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Jul 29, 2020Group: Advisory / Data collection ...Advisory / Data collection / Derived calculations / Structure summary
Category: chem_comp / database_PDB_caveat ...chem_comp / database_PDB_caveat / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.mon_nstd_flag / _chem_comp.name ..._chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: inducible nitric oxide synthase
B: inducible nitric oxide synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)103,03211
Polymers100,4162
Non-polymers2,6169
Water4,558253
1
A: inducible nitric oxide synthase
hetero molecules

A: inducible nitric oxide synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)102,86412
Polymers100,4162
Non-polymers2,44810
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation11_655-x+y+1,y,-z+1/21
Buried area9820 Å2
ΔGint-47 kcal/mol
Surface area34300 Å2
MethodPISA, PQS
2
B: inducible nitric oxide synthase
hetero molecules

B: inducible nitric oxide synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)103,20010
Polymers100,4162
Non-polymers2,7848
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation9_766-x+2,-x+y+1,-z+5/31
Buried area9670 Å2
ΔGint-54 kcal/mol
Surface area33910 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)214.422, 214.422, 113.267
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number178
Space group name H-MP6122
Components on special symmetry positions
IDModelComponents
11A-1093-

HOH

21A-1169-

HOH

31A-1173-

HOH

41B-1088-

HOH

51B-1089-

HOH

61B-1133-

HOH

71B-1233-

HOH

DetailsTo get one biological dimer apply the following transformation to chain A: 1+y-x,y,1/2-z / To get another biological dimer, apply the following transformation to chain B: 2-x,1-x+y,2/3-z+5/3

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Components

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Protein / Sugars , 2 types, 3 molecules AB

#1: Protein inducible nitric oxide synthase / Nitric oxide synthase / NOS / type II / Inducible NOS / iNOS / Macrophage NOS / MAC-NOS


Mass: 50208.027 Da / Num. of mol.: 2 / Fragment: oxygenase domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: iNOS / Plasmid: PCWORI / Production host: Escherichia coli (E. coli) / References: UniProt: P29477, nitric-oxide synthase (NADPH)
#6: Sugar ChemComp-BOG / octyl beta-D-glucopyranoside / Octyl glucoside


Type: D-saccharide / Mass: 292.369 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C14H28O6 / Comment: detergent*YM
IdentifierTypeProgram
b-octylglucosideIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0

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Non-polymers , 5 types, 261 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-INE / 3-BROMO-7-NITROINDAZOLE


Mass: 242.030 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C7H4BrN3O2
#5: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 253 / 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: 3.74 Å3/Da / Density % sol: 67.12 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6
Details: Lithium Sulfate, B-octyl-glucodise, MES buffer, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 0.974 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Aug 25, 2002
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.974 Å / Relative weight: 1
ReflectionResolution: 2.4→20 Å / Num. all: 59481 / Num. obs: 59481 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Biso Wilson estimate: 40.7 Å2 / Rmerge(I) obs: 0.07 / Rsym value: 0.07 / Net I/σ(I): 20.6
Reflection shellResolution: 2.4→2.49 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.33 / Mean I/σ(I) obs: 3.6 / Num. unique all: 5605 / Rsym value: 0.33 / % possible all: 95.2

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Processing

Software
NameClassification
DENZOdata reduction
SCALEPACKdata scaling
CNSrefinement
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→19.94 Å / Rfactor Rfree error: 0.005 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.284 2993 5 %RANDOM
Rwork0.25 ---
all-59331 --
obs-59331 98.9 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 27.1981 Å2 / ksol: 0.313111 e/Å3
Displacement parametersBiso mean: 55.6 Å2
Baniso -1Baniso -2Baniso -3
1--18.43 Å2-8.49 Å20 Å2
2---18.43 Å20 Å2
3---36.85 Å2
Refine analyzeLuzzati coordinate error free: 0.45 Å / Luzzati sigma a free: 0.63 Å
Refinement stepCycle: LAST / Resolution: 2.4→19.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6716 0 174 253 7143
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.008
X-RAY DIFFRACTIONc_angle_deg1.3
X-RAY DIFFRACTIONc_dihedral_angle_d23.1
X-RAY DIFFRACTIONc_improper_angle_d1.22
X-RAY DIFFRACTIONc_mcbond_it1.41.5
X-RAY DIFFRACTIONc_mcangle_it2.392
X-RAY DIFFRACTIONc_scbond_it1.962
X-RAY DIFFRACTIONc_scangle_it3.032.5
LS refinement shellResolution: 2.4→2.55 Å / Rfactor Rfree error: 0.021 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.442 455 4.8 %
Rwork0.401 8991 -
obs-5605 96.2 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PARHCSDX.PROTOPHCSDX.PRO
X-RAY DIFFRACTION2PARAM19.SOLTOPH19.SOL
X-RAY DIFFRACTION3PARAM19X.HEMETOPH19X.HEME
X-RAY DIFFRACTION43BR7NI.PAR3BR7NI.TOP
X-RAY DIFFRACTION5MISC.PARMISC.TOP

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