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Yorodumi- PDB-4cx7: Structure of human iNOS heme domain in complex with (R)-6-(3-AMIN... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4cx7 | ||||||
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Title | Structure of human iNOS heme domain in complex with (R)-6-(3-AMINO-2-(5-(2-(6-AMINO-4- METHYLPYRIDIN-2-YL)ETHYL)PYRIDIN-3-YL)PROPYL)-4- METHYLPYRIDIN-2-AMINE | ||||||
Components | NITRIC OXIDE SYNTHASE, INDUCIBLE | ||||||
Keywords | OXIDOREDUCTASE / INHIBITOR COMPLEX | ||||||
Function / homology | Function and homology information positive regulation of leukocyte mediated cytotoxicity / Inhibition of nitric oxide production / Nitric oxide stimulates guanylate cyclase / prostaglandin secretion / positive regulation of killing of cells of another organism / ROS and RNS production in phagocytes / regulation of cellular respiration / tetrahydrobiopterin binding / arginine binding / cortical cytoskeleton ...positive regulation of leukocyte mediated cytotoxicity / Inhibition of nitric oxide production / Nitric oxide stimulates guanylate cyclase / prostaglandin secretion / positive regulation of killing of cells of another organism / ROS and RNS production in phagocytes / regulation of cellular respiration / tetrahydrobiopterin binding / arginine binding / cortical cytoskeleton / superoxide metabolic process / regulation of cytokine production involved in inflammatory response / peptidyl-cysteine S-nitrosylation / peroxisomal matrix / regulation of insulin secretion / nitric-oxide synthase (NADPH) / nitric-oxide synthase activity / nitric oxide mediated signal transduction / arginine catabolic process / nitric oxide biosynthetic process / negative regulation of blood pressure / response to hormone / cell redox homeostasis / innate immune response in mucosa / positive regulation of interleukin-8 production / Peroxisomal protein import / response to bacterium / negative regulation of protein catabolic process / cellular response to type II interferon / peroxisome / positive regulation of interleukin-6 production / circadian rhythm / cellular response to xenobiotic stimulus / FMN binding / flavin adenine dinucleotide binding / NADP binding / regulation of cell population proliferation / Interleukin-4 and Interleukin-13 signaling / cellular response to lipopolysaccharide / defense response to Gram-negative bacterium / response to lipopolysaccharide / response to hypoxia / calmodulin binding / defense response to bacterium / inflammatory response / negative regulation of gene expression / heme binding / perinuclear region of cytoplasm / protein homodimerization activity / nucleoplasm / metal ion binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.16 Å | ||||||
Authors | Li, H. / Poulos, T.L. | ||||||
Citation | Journal: Biochemistry / Year: 2014 Title: Mobility of a Conserved Tyrosine Residue Controls Isoform-Dependent Enzyme-Inhibitor Interactions in Nitric Oxide Synthases. Authors: Li, H. / Jamal, J. / Delker, S.L. / Plaza, C. / Ji, H. / Jing, Q. / Huang, H. / Kang, S. / Silverman, R.B. / Poulos, T.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4cx7.cif.gz | 691.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4cx7.ent.gz | 579.5 KB | Display | PDB format |
PDBx/mmJSON format | 4cx7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cx/4cx7 ftp://data.pdbj.org/pub/pdb/validation_reports/cx/4cx7 | HTTPS FTP |
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-Related structure data
Related structure data | 4cwvC 4cwwC 4cwxC 4cwyC 4cwzC 4cx0C 4cx1C 4cx2C 4cx3C 4cx4C 4cx5C 4cx6C 1nsiS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Beg auth comp-ID: ARG / Beg label comp-ID: ARG / End auth comp-ID: GLN / End label comp-ID: GLN / Refine code: 4 / Auth seq-ID: 83 - 502 / Label seq-ID: 10 - 429
NCS ensembles :
NCS oper:
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-Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 49705.531 Da / Num. of mol.: 4 / Fragment: HEME DOMAIN, RESIDUES 74-504 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P35228, nitric-oxide synthase (NADPH) |
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-Non-polymers , 5 types, 25 molecules
#2: Chemical | ChemComp-HEM / #3: Chemical | ChemComp-H4B / #4: Chemical | ChemComp-S71 / ( #5: Chemical | ChemComp-GOL / #6: Chemical | ChemComp-SO4 / |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 5.4 Å3/Da / Density % sol: 77.3 % Description: R-MERGE 0.23 R-PIM 0.07 CC ONE-HALF 99.6 HIGHEST RESOLUTION SHELL R-MERGE 1.863 R-PIM 0.582 CC ONE-HALF 49.3 |
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Crystal grow | pH: 6 Details: 1.3M AMMONIUM SULFATE, 50 MM NA CITRATE, PH5.0 30% GLYCEROL 5 MM GSH, pH 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.979 |
Detector | Type: DECTRIS PILATUS / Detector: PIXEL / Date: Jul 29, 2013 / Details: MIRRORS |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 3.16→50 Å / Num. obs: 72855 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 11.9 % / Rmerge(I) obs: 0.23 / Net I/σ(I): 12.6 |
Reflection shell | Resolution: 3.16→3.33 Å / Redundancy: 10.9 % / Rmerge(I) obs: 1.5 / Mean I/σ(I) obs: 1.5 / % possible all: 98.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1NSI Resolution: 3.16→146.83 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.932 / SU B: 32.488 / SU ML: 0.256 / Cross valid method: THROUGHOUT / ESU R: 0.568 / ESU R Free: 0.312 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED FRAGMENT (RESIDUES 108 TO 114 IN EACH CHAIN) AROUND THE ZN BINDING SITE IS DISORDERED.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 78.317 Å2
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Refinement step | Cycle: LAST / Resolution: 3.16→146.83 Å
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Refine LS restraints |
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