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- PDB-1noc: MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 11... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1noc | ||||||
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Title | MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114) COMPLEXED WITH TYPE I E. COLI CHLORAMPHENICOL ACETYL TRANSFERASE AND IMIDAZOLE | ||||||
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![]() | COMPLEX (OXIDOREDUCTASE/TRANSFERASE) / NITRIC OXIDE / L-ARGININE MONOOXYGENASE / HEME / IMIDAZOLE / NOS / NO / CAT / COMPLEX (OXIDOREDUCTASE-TRANSFERASE) / COMPLEX (OXIDOREDUCTASE-TRANSFERASE) complex | ||||||
Function / homology | ![]() chloramphenicol O-acetyltransferase activity / chloramphenicol O-acetyltransferase / 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 ...chloramphenicol O-acetyltransferase activity / chloramphenicol O-acetyltransferase / 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 / cGMP-mediated signaling / nitric-oxide synthase binding / regulation of cytokine production involved in inflammatory response / peptidyl-cysteine S-nitrosylation / cellular response to cytokine stimulus / regulation of insulin secretion / cellular response to organic cyclic compound / nitric-oxide synthase (NADPH) / blood vessel remodeling / nitric oxide mediated signal transduction / response to tumor necrosis factor / nitric-oxide synthase activity / arginine catabolic process / nitric oxide biosynthetic process / negative regulation of blood pressure / response to hormone / positive regulation of interleukin-8 production / response to bacterium / Hsp90 protein binding / negative regulation of protein catabolic process / beta-catenin binding / regulation of blood pressure / cellular response to type II interferon / circadian rhythm / peroxisome / positive regulation of interleukin-6 production / cellular response to xenobiotic stimulus / FMN binding / NADP binding / actin binding / regulation of cell population proliferation / flavin adenine dinucleotide binding / cellular response to lipopolysaccharide / response to lipopolysaccharide / calmodulin binding / response to hypoxia / intracellular signal transduction / defense response to bacterium / cadherin binding / inflammatory response / positive regulation of apoptotic process / negative regulation of gene expression / response to antibiotic / heme binding / protein kinase binding / perinuclear region of cytoplasm / protein homodimerization activity / extracellular space / identical protein binding / nucleus / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Crane, B.R. / Arvai, A.S. / Getzoff, E.D. / Stuehr, D.J. / Tainer, J.A. | ||||||
![]() | ![]() Title: The structure of nitric oxide synthase oxygenase domain and inhibitor complexes. Authors: Crane, B.R. / Arvai, A.S. / Gachhui, R. / Wu, C. / Ghosh, D.K. / Getzoff, E.D. / Stuehr, D.J. / Tainer, J.A. #1: ![]() Title: Characterization of the Inducible Nitric Oxide Synthase Oxygenase Domain Identifies a 49 Amino Acid Segment Required for Subunit Dimerization and Tetrahydrobiopterin Interaction Authors: Ghosh, D.K. / Wu, C. / Pitters, E. / Moloney, M. / Werner, E.R. / Mayer, B. / Stuehr, D.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 138.2 KB | Display | ![]() |
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PDB format | ![]() | 105.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 491.3 KB | Display | ![]() |
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Full document | ![]() | 502.8 KB | Display | |
Data in XML | ![]() | 14.7 KB | Display | |
Data in CIF | ![]() | 22.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 45139.184 Da / Num. of mol.: 1 / Fragment: OXYGENASE DOMAIN 115-498 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Protein | Mass: 25692.145 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: P62577, chloramphenicol O-acetyltransferase | ||||
#3: Chemical | ChemComp-HEM / | ||||
#4: Chemical | #5: Water | ChemComp-HOH / | Nonpolymer details | TWO IMIDAZOLE MOLECULES BIND IN THE INOS ACTIVE CENTER: IMI 901 BINDS THE HEME IRON, WHEREAS IMI ...TWO IMIDAZOLE MOLECULES BIND IN THE INOS ACTIVE CENTER: IMI 901 BINDS THE HEME IRON, WHEREAS IMI 902 HYDROGEN-BONDS TO GLU 371. | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.8 Å3/Da / Density % sol: 68 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 1, 1997 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→30 Å / Num. obs: 32117 / % possible obs: 98.9 % / Observed criterion σ(I): 0 / Redundancy: 7.1 % / Rsym value: 0.059 / Net I/σ(I): 30.6 |
Reflection shell | Resolution: 2.6→2.7 Å / Mean I/σ(I) obs: 2.9 / Rsym value: 0.31 / % possible all: 92 |
Reflection | *PLUS Rmerge(I) obs: 0.059 / Num. measured all: 226448 |
Reflection shell | *PLUS % possible obs: 92 % / Rmerge(I) obs: 0.31 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 66.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati d res low obs: 6 Å / Luzzati sigma a obs: 0.35 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→2.7 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.7 Å / Total num. of bins used: 8
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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