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- PDB-3hr4: Human iNOS Reductase and Calmodulin Complex -

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Basic information

Entry
Database: PDB / ID: 3hr4
TitleHuman iNOS Reductase and Calmodulin Complex
Components
  • Calmodulin
  • Nitric oxide synthase, inducible
KeywordsOxidoreductase/METAL BINDING PROTEIN / inducible nitric oxide synthase / NOS / iNOS / calmodulin / Calmodulin-binding / FAD / FMN / Heme / Iron / Metal-binding / NADP / Oxidoreductase / Phosphoprotein / Isopeptide bond / Methylation / Oxidoreductase-METAL BINDING PROTEIN COMPLEX
Function / homology
Function and homology information


positive regulation of leukocyte mediated cytotoxicity / Inhibition of nitric oxide production / peptidyl-cysteine S-nitrosylation / : / : / : / : / : / positive regulation of protein autophosphorylation / negative regulation of peptidyl-threonine phosphorylation ...positive regulation of leukocyte mediated cytotoxicity / Inhibition of nitric oxide production / peptidyl-cysteine S-nitrosylation / : / : / : / : / : / positive regulation of protein autophosphorylation / negative regulation of peptidyl-threonine phosphorylation / regulation of cellular respiration / Nitric oxide stimulates guanylate cyclase / establishment of protein localization to mitochondrial membrane / prostaglandin secretion / type 3 metabotropic glutamate receptor binding / ROS and RNS production in phagocytes / tetrahydrobiopterin binding / arginine binding / CaM pathway / positive regulation of peptidyl-threonine phosphorylation / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events / positive regulation of DNA binding / Reduction of cytosolic Ca++ levels / Activation of Ca-permeable Kainate Receptor / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / response to corticosterone / CaMK IV-mediated phosphorylation of CREB / PKA activation / negative regulation of high voltage-gated calcium channel activity / Glycogen breakdown (glycogenolysis) / CLEC7A (Dectin-1) induces NFAT activation / superoxide metabolic process / Activation of RAC1 downstream of NMDARs / negative regulation of ryanodine-sensitive calcium-release channel activity / organelle localization by membrane tethering / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / negative regulation of calcium ion export across plasma membrane / regulation of cardiac muscle cell action potential / regulation of cytokine production involved in inflammatory response / presynaptic endocytosis / nitric-oxide synthase binding / Synthesis of IP3 and IP4 in the cytosol / cortical cytoskeleton / regulation of synaptic vesicle exocytosis / regulation of cell communication by electrical coupling involved in cardiac conduction / Fc-gamma receptor signaling pathway involved in phagocytosis / Phase 0 - rapid depolarisation / calcineurin-mediated signaling / Negative regulation of NMDA receptor-mediated neuronal transmission / Unblocking of NMDA receptors, glutamate binding and activation / RHO GTPases activate PAKs / peroxisomal matrix / Ion transport by P-type ATPases / Uptake and function of anthrax toxins / adenylate cyclase binding / regulation of ryanodine-sensitive calcium-release channel activity / protein phosphatase activator activity / Long-term potentiation / nitric oxide mediated signal transduction / Calcineurin activates NFAT / Regulation of MECP2 expression and activity / positive regulation of protein serine/threonine kinase activity / nitric-oxide synthase (NADPH) / DARPP-32 events / catalytic complex / Smooth Muscle Contraction / detection of calcium ion / regulation of synaptic vesicle endocytosis / regulation of cardiac muscle contraction / nitric-oxide synthase activity / L-arginine catabolic process / RHO GTPases activate IQGAPs / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / activation of adenylate cyclase activity / cellular response to interferon-beta / Protein methylation / phosphatidylinositol 3-kinase binding / calcium channel inhibitor activity / Activation of AMPK downstream of NMDARs / presynaptic cytosol / negative regulation of blood pressure / positive regulation of nitric-oxide synthase activity / Ion homeostasis / response to hormone / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / enzyme regulator activity / eNOS activation / titin binding / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / sperm midpiece / regulation of calcium-mediated signaling / nitric oxide biosynthetic process / voltage-gated potassium channel complex / calcium channel complex / FCERI mediated Ca+2 mobilization
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #410 / Flavodoxin domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Nitric-oxide synthase, eukaryote / Nitric oxide synthase, N-terminal / Nitric oxide synthase, N-terminal domain superfamily / Nitric oxide synthase, domain 2 superfamily / Nitric oxide synthase, domain 1 superfamily / Nitric oxide synthase, domain 3 superfamily / : ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #410 / Flavodoxin domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Nitric-oxide synthase, eukaryote / Nitric oxide synthase, N-terminal / Nitric oxide synthase, N-terminal domain superfamily / Nitric oxide synthase, domain 2 superfamily / Nitric oxide synthase, domain 1 superfamily / Nitric oxide synthase, domain 3 superfamily / : / Nitric oxide synthase, oxygenase domain / Nitric oxide synthase (NOS) signature. / 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 / Flavodoxin-like domain profile. / Flavodoxin/nitric oxide synthase / Oxidoreductase FAD/NAD(P)-binding / Oxidoreductase NAD-binding domain / FAD-binding domain, ferredoxin reductase-type / Ferredoxin-NADP reductase (FNR), nucleotide-binding domain / Ferredoxin reductase-type FAD binding domain profile. / Riboflavin synthase-like beta-barrel / Flavoprotein-like superfamily / Helix non-globular / EF-hand domain pair / Special / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
FLAVIN MONONUCLEOTIDE / Calmodulin-1 / Nitric oxide synthase, inducible / Calmodulin-3
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsXia, C. / Misra, I. / Iyanaki, T. / Kim, J.J.K.
CitationJournal: J.Biol.Chem. / Year: 2009
Title: Regulation of Interdomain Interactions by CaM in Inducible Nitric Oxide Synthase
Authors: Xia, C. / Misra, I. / Iyanaki, T. / Kim, J.J.K.
History
DepositionJun 8, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 8, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 5, 2012Group: Derived calculations
Revision 1.3Mar 7, 2018Group: Data collection / Category: diffrn_source / Item: _diffrn_source.source
Revision 1.4Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _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_asym_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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Nitric oxide synthase, inducible
B: Calmodulin
C: Nitric oxide synthase, inducible
D: Calmodulin
E: Nitric oxide synthase, inducible
F: Calmodulin
G: Nitric oxide synthase, inducible
H: Calmodulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)170,05728
Polymers167,5908
Non-polymers2,46720
Water1,27971
1
A: Nitric oxide synthase, inducible
B: Calmodulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,5147
Polymers41,8982
Non-polymers6175
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3510 Å2
ΔGint-36 kcal/mol
Surface area16400 Å2
2
C: Nitric oxide synthase, inducible
D: Calmodulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,5147
Polymers41,8982
Non-polymers6175
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
E: Nitric oxide synthase, inducible
F: Calmodulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,5147
Polymers41,8982
Non-polymers6175
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
G: Nitric oxide synthase, inducible
H: Calmodulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,5147
Polymers41,8982
Non-polymers6175
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)36.600, 160.840, 127.770
Angle α, β, γ (deg.)90.00, 90.37, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
Nitric oxide synthase, inducible / Inducible NO synthase / Inducible NOS / iNOS / NOS type II / Hepatocyte NOS / HEP-NOS


Mass: 25045.004 Da / Num. of mol.: 4 / Fragment: Residues 503-715
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: Calmodulin, Inducible Nitric Oxide Synthase, NOS2, NOS2A
Plasmid: PCWORI+ / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P35228, nitric-oxide synthase (NADPH)
#2: Protein
Calmodulin / CaM


Mass: 16852.545 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2, CAM3, CAMC, CAMIII
Plasmid: pKK-CaM / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P62158, UniProt: P0DP23*PLUS
#3: Chemical
ChemComp-FMN / FLAVIN MONONUCLEOTIDE / RIBOFLAVIN MONOPHOSPHATE


Mass: 456.344 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C17H21N4O9P
#4: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: Ca
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 71 / 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: 2.24 Å3/Da / Density % sol: 45.19 %
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop / pH: 5
Details: PEG 8K, SODIUM ACETATE, SODIUM CHLORATE, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-007 / Wavelength: 1.5418 Å
DetectorType: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Sep 27, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.5→29.69 Å / Num. obs: 48283 / % possible obs: 94.6 % / Redundancy: 2.7 % / Biso Wilson estimate: 60.9 Å2 / Rmerge(I) obs: 0.065 / Net I/σ(I): 15.5

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
CNS1.2refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1TLL, 1NIW, 1FOT

1tll

1niw

1fot


Resolution: 2.5→29.69 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 428243.6 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Details: BULK SOLVENT MODEL USED
RfactorNum. reflection% reflectionSelection details
Rfree0.309 2414 5 %RANDOM
Rwork0.237 ---
obs0.237 48283 94.6 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 32.8557 Å2 / ksol: 0.3 e/Å3
Displacement parametersBiso mean: 64.4 Å2
Baniso -1Baniso -2Baniso -3
1-11.64 Å20 Å23.21 Å2
2--12.86 Å20 Å2
3----24.5 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.53 Å0.39 Å
Luzzati d res low-30 Å
Luzzati sigma a0.55 Å0.48 Å
Refinement stepCycle: LAST / Resolution: 2.5→29.69 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10383 0 140 71 10594
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_d21.3
X-RAY DIFFRACTIONc_improper_angle_d0.9
X-RAY DIFFRACTIONc_mcbond_it1.41.5
X-RAY DIFFRACTIONc_mcangle_it2.42
X-RAY DIFFRACTIONc_scbond_it1.872
X-RAY DIFFRACTIONc_scangle_it2.872.5
LS refinement shellResolution: 2.5→2.66 Å / Rfactor Rfree error: 0.023 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.411 309 5 %
Rwork0.382 5888 -
obs--73.1 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1protein_rep.paramprotein.top
X-RAY DIFFRACTION2cofac_fmcofac_fm
X-RAY DIFFRACTION3water_rep.paramwater_rep.top
X-RAY DIFFRACTION4ion.paramion.top

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