+Open data
-Basic information
Entry | Database: PDB / ID: 2nse | ||||||
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Title | BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE SUBSTRATE COMPLEX | ||||||
Components | NITRIC OXIDE SYNTHASE | ||||||
Keywords | COMPLEX (OXIDOREDUCTASE/PEPTIDE) / NITRIC OXIDE SYNTHASE / ARGININE / HEME PROTEIN / TETRAHYDROBIOPTERIN / COMPLEX (OXIDOREDUCTASE-PEPTIDE) / COMPLEX (OXIDOREDUCTASE-PEPTIDE) complex | ||||||
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 mediated signal transduction / nitric-oxide synthase activity / arginine catabolic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / nitric oxide biosynthetic process / 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 mediated signal transduction / nitric-oxide synthase activity / arginine catabolic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / nitric oxide biosynthetic process / negative regulation of blood pressure / response to hormone / mitochondrion organization / caveola / blood coagulation / FMN binding / NADP binding / flavin adenine dinucleotide binding / response to lipopolysaccharide / calmodulin binding / cytoskeleton / heme binding / Golgi apparatus / nucleus / metal ion binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD, MIRAS / Resolution: 2.34 Å | ||||||
Authors | Raman, C.S. / Li, H. / Martasek, P. / Kral, V. / Masters, B.S.S. / Poulos, T.L. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1998 Title: Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center. Authors: Raman, C.S. / Li, H. / Martasek, P. / Kral, V. / Masters, B.S. / Poulos, T.L. #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. #2: Journal: Science / Year: 1997 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2nse.cif.gz | 188.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2nse.ent.gz | 147.2 KB | Display | PDB format |
PDBx/mmJSON format | 2nse.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2nse_validation.pdf.gz | 589.8 KB | Display | wwPDB validaton report |
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Full document | 2nse_full_validation.pdf.gz | 610.6 KB | Display | |
Data in XML | 2nse_validation.xml.gz | 20.8 KB | Display | |
Data in CIF | 2nse_validation.cif.gz | 31.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ns/2nse ftp://data.pdbj.org/pub/pdb/validation_reports/ns/2nse | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.283947, -0.941706, 0.180452), Vector: |
-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 49710.105 Da / Num. of mol.: 2 / Fragment: HEME DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Cell: ENDOTHELIAL / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P29473, nitric-oxide synthase (NADPH) |
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-Non-polymers , 7 types, 271 molecules
#2: Chemical | #3: Chemical | #4: Chemical | #5: Chemical | #6: Chemical | ChemComp-ZN / | #7: Chemical | ChemComp-GOL / | #8: Water | ChemComp-HOH / | |
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-Details
Nonpolymer details | ARG C 700 AND ARG D 700 ARE SUBSTRATES |
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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: 2.5 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.5 | ||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL1-5 / Wavelength: 0.9801 |
Detector | Type: ADSC / Detector: CCD / Date: Feb 1, 1998 / Details: MIRROR |
Radiation | Monochromator: YES / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9801 Å / Relative weight: 1 |
Reflection | Resolution: 2.34→30 Å / Num. obs: 40100 / % possible obs: 96.2 % / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Rsym value: 0.048 / Net I/σ(I): 16.9 |
Reflection shell | Resolution: 2.34→2.4 Å / Redundancy: 2.5 % / Mean I/σ(I) obs: 3.2 / Rsym value: 0.121 / % possible all: 79.5 |
Reflection | *PLUS Num. measured all: 131275 / Rmerge(I) obs: 0.048 |
Reflection shell | *PLUS % possible obs: 79.5 % / Rmerge(I) obs: 0.121 |
-Processing
Software |
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Refinement | Method to determine structure: MAD, MIRAS / Resolution: 2.34→30 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Cross valid method: FREE R / σ(F): 2 Details: NCS RESTRAINTS WERE IMPOSED AT THE EARLY STAGE OF REFINEMENT. SEPARATE PARAMETER FILES WERE USED FOR ARG 700 TO DEFINE THE CARBOXYLIC GROUP INSTEAD OF THE CARBONYL GROUP.
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Refinement step | Cycle: LAST / Resolution: 2.34→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.34→2.45 Å / Total num. of bins used: 8
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Xplor file |
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