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Yorodumi- PDB-3e7s: Structure of bovine eNOS oxygenase domain with inhibitor AR-C95791 -
+Open data
-Basic information
Entry | Database: PDB / ID: 3e7s | ||||||
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Title | Structure of bovine eNOS oxygenase domain with inhibitor AR-C95791 | ||||||
Components | (Nitric oxide synthase, ...) x 2 | ||||||
Keywords | OXIDOREDUCTASE / NITRIC OXIDE SYNTHASE / NOS / HEME / TETRAHYDROBIOPTERIN / OXIDOREDUCTASE Calmodulin-binding / FAD / FMN / Iron / Metal-binding / NADP / Polymorphism / Zinc | ||||||
Function / homology | Function and homology information cellular response to laminar fluid shear stress / positive regulation of guanylate cyclase activity / negative regulation of leukocyte cell-cell adhesion / nitric-oxide synthase (NADPH) / nitric-oxide synthase activity / nitric oxide mediated signal transduction / arginine catabolic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / mitochondrion organization / negative regulation of blood pressure ...cellular response to laminar fluid shear stress / positive regulation of guanylate cyclase activity / negative regulation of leukocyte cell-cell adhesion / nitric-oxide synthase (NADPH) / nitric-oxide synthase activity / nitric oxide mediated signal transduction / arginine catabolic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / mitochondrion organization / negative regulation of blood pressure / nitric oxide biosynthetic process / response to hormone / caveola / blood coagulation / FMN binding / flavin adenine dinucleotide binding / NADP binding / response to lipopolysaccharide / cytoskeleton / calmodulin binding / heme binding / Golgi apparatus / metal ion binding / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Garcin, E.D. / Arvai, A.S. / Rosenfeld, R.J. / Kroeger, M.D. / Crane, B.R. / Andersson, G. / Andrews, G. / Hamley, P.J. / Mallinder, P.R. / Nicholls, D.J. ...Garcin, E.D. / Arvai, A.S. / Rosenfeld, R.J. / Kroeger, M.D. / Crane, B.R. / Andersson, G. / Andrews, G. / Hamley, P.J. / Mallinder, P.R. / Nicholls, D.J. / St-Gallay, S.A. / Tinker, A.C. / Gensmantel, N.P. / Mete, A. / Cheshire, D.R. / Connolly, S. / Stuehr, D.J. / Aberg, A. / Wallace, A.V. / Tainer, J.A. / Getzoff, E.D. | ||||||
Citation | Journal: Nat.Chem.Biol. / Year: 2008 Title: Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase. Authors: Garcin, E.D. / Arvai, A.S. / Rosenfeld, R.J. / Kroeger, M.D. / Crane, B.R. / Andersson, G. / Andrews, G. / Hamley, P.J. / Mallinder, P.R. / Nicholls, D.J. / St-Gallay, S.A. / Tinker, A.C. / ...Authors: Garcin, E.D. / Arvai, A.S. / Rosenfeld, R.J. / Kroeger, M.D. / Crane, B.R. / Andersson, G. / Andrews, G. / Hamley, P.J. / Mallinder, P.R. / Nicholls, D.J. / St-Gallay, S.A. / Tinker, A.C. / Gensmantel, N.P. / Mete, A. / Cheshire, D.R. / Connolly, S. / Stuehr, D.J. / Aberg, A. / Wallace, A.V. / Tainer, J.A. / Getzoff, E.D. | ||||||
History |
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Remark 999 | SEQUENCE BASED ON THE CLEAR ELECTRON DENSITY AND SEQUENCE ALIGNMENTS SHOWING AN ARG RESIDUE AT ... SEQUENCE BASED ON THE CLEAR ELECTRON DENSITY AND SEQUENCE ALIGNMENTS SHOWING AN ARG RESIDUE AT THIS POSITION IN OTHER ISOFORMS, THE AUTHORS CONFIRM THAT RESIDUE 97 IS AN ARG AND NOT A CYS |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3e7s.cif.gz | 181.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3e7s.ent.gz | 141.4 KB | Display | PDB format |
PDBx/mmJSON format | 3e7s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e7/3e7s ftp://data.pdbj.org/pub/pdb/validation_reports/e7/3e7s | HTTPS FTP |
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-Related structure data
Related structure data | 3e65C 3e67C 3e68C 3e6lC 3e6nC 3e6oC 3e6tC 3e7gC 3e7iC 3e7mC 3e7tC 3eahC 3eaiC 3ebdC 3ebfC 3ej8C C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Nitric oxide synthase, ... , 2 types, 2 molecules AB
#1: Protein | Mass: 48393.703 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: no chemical modification of the Cys381 / Source: (gene. exp.) Bos taurus (cattle) / Gene: Nos3 / Plasmid: PCWORI / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P29473, nitric-oxide synthase (NADPH) |
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#2: Protein | Mass: 48497.688 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: the Cys381 is chemically modified / Source: (gene. exp.) Bos taurus (cattle) / Gene: Nos3 / Plasmid: PCWORI / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P29473, nitric-oxide synthase (NADPH) |
-Non-polymers , 4 types, 174 molecules
#3: Chemical | ChemComp-ZN / | ||||
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#4: Chemical | #5: Chemical | ChemComp-AT2 / #6: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.54 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6 Details: MAGNESIUM ACETATE, SODIUM CACODYLATE, TCEP, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.08 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→30 Å / Num. obs: 29456 / % possible obs: 86 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.084 / Rsym value: 0.084 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.5→30 Å / Occupancy max: 1 / Occupancy min: 1 / Data cutoff high absF: 0 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Bsol: 22.51 Å2 | ||||||||||||||||||||
Displacement parameters | Biso max: 83.62 Å2 / Biso mean: 28.016 Å2 / Biso min: 2.8 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→30 Å
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Refine LS restraints |
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