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- PDB-2cnd: STRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE O... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2cnd | |||||||||
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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 | |||||||||
![]() | NADH-DEPENDENT NITRATE REDUCTASE | |||||||||
![]() | OXIDOREDUCTASE / NITRATE ASSIMILATING ENZYME / NITROGENOUS ACCEPTOR | |||||||||
Function / homology | ![]() 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 | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Lu, G. / Lindqvist, Y. / Schneider, G. | |||||||||
![]() | ![]() 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: ![]() 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: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 67.8 KB | Display | ![]() |
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PDB format | ![]() | 49.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 464.2 KB | Display | ![]() |
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Full document | ![]() | 476.3 KB | Display | |
Data in XML | ![]() | 8.9 KB | Display | |
Data in CIF | ![]() | 12.8 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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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 115 / 2: CIS PROLINE - PRO 163 |
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Components
#1: Protein | Mass: 30590.322 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-FAD / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.15 Å3/Da / Density % sol: 60.93 % |
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-Data collection
Reflection | Num. obs: 10519 / % possible obs: 81 % / Observed criterion σ(I): 1 |
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Reflection | *PLUS Highest resolution: 2.5 Å / Redundancy: 5.4 % / Num. measured all: 57374 / Rmerge(I) obs: 0.063 |
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Processing
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Refinement | Resolution: 2.5→6.5 Å / σ(F): 1
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Displacement parameters | Biso mean: 35 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→6.5 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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