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Yorodumi- PDB-1cnf: STRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE O... -
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-Basic information
Entry | Database: PDB / ID: 1cnf | ||||||
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Title | STRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE OF THE CYTOCHROME B REDUCTASE FRAGMENT AT 2.5 ANGSTROMS, ITS ADP COMPLEX AND AN ACTIVE SITE MUTANT AND MODELING OF THE CYTOCHROME B DOMAIN | ||||||
Components | NITRATE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / NITROGENOUS ACCEPTOR / NITRATE ASSIMILATING ENZYME | ||||||
Function / homology | Function and homology information nitrate reductase (NADH) / nitrate reductase (NADH) activity / molybdenum ion binding / nitrate assimilation / nitric oxide biosynthetic process / FAD binding / heme binding Similarity search - Function | ||||||
Biological species | Zea mays (maize) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.7 Å | ||||||
Authors | Lu, G. / Lindqvist, Y. / Schneider, G. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 A, its ADP complex and an active-site mutant and modeling of the cytochrome b domain. Authors: Lu, G. / Lindqvist, Y. / Schneider, G. / Dwivedi, U. / Campbell, W. #1: Journal: To be Published Title: A Method for Processing Diffraction Data from Twinned Crystals and its Application in the Structure Determination of a Fad(Slash)Nadh Binding Fragment of Nitrate Reductase Authors: Lu, G. / Lindqvist, Y. / Schneider, G. #2: Journal: Structure / Year: 1995 Title: Crystal Structure of the Fad Containing Fragment of Corn Nitrate Reductase at 2.5 Angstroms Resolution: Relationship to Other Flavoprotein Reductase Authors: Lu, G. / Campbell, W. / Lindqvist, Y. / Schneider, G. #3: Journal: J.Mol.Biol. / Year: 1992 Title: Crystallization and Preliminary Crystallographic Studies of the Fad Domain of Corn Nadh:Nitrate Reductase Authors: Lu, G. / Campbell, W. / Lindqvist, Y. / Schneider, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cnf.cif.gz | 62 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cnf.ent.gz | 45.3 KB | Display | PDB format |
PDBx/mmJSON format | 1cnf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1cnf_validation.pdf.gz | 527.1 KB | Display | wwPDB validaton report |
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Full document | 1cnf_full_validation.pdf.gz | 544 KB | Display | |
Data in XML | 1cnf_validation.xml.gz | 10.2 KB | Display | |
Data in CIF | 1cnf_validation.cif.gz | 13.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cn/1cnf ftp://data.pdbj.org/pub/pdb/validation_reports/cn/1cnf | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 115 / 2: CIS PROLINE - PRO 163 |
-Components
#1: Protein | Mass: 30590.322 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Zea mays (maize) / Organ: LEAF / References: UniProt: P17571, EC: 1.6.6.1 |
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#2: Chemical | ChemComp-FAD / |
#3: Chemical | ChemComp-ADP / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.15 Å3/Da / Density % sol: 60.93 % |
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 8225 / % possible obs: 81 % / Observed criterion σ(I): 1 |
Reflection | *PLUS Highest resolution: 2.7 Å / Redundancy: 2.4 % / Num. measured all: 20157 / Rmerge(I) obs: 0.062 |
-Processing
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Refinement | Resolution: 2.7→8 Å / σ(F): 1
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Displacement parameters | Biso mean: 33 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→8 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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