[English] 日本語
![](img/lk-miru.gif)
- PDB-1cnf: STRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE O... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1cnf | ||||||
---|---|---|---|---|---|---|---|
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 | ||||||
![]() | NITRATE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / NITROGENOUS ACCEPTOR / NITRATE ASSIMILATING ENZYME | ||||||
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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 62 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 45.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 527.1 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 544 KB | Display | |
Data in XML | ![]() | 10.2 KB | Display | |
Data in CIF | ![]() | 13.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
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.) ![]() ![]() |
---|---|
#2: Chemical | ChemComp-FAD / |
#3: Chemical | ChemComp-ADP / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.15 Å3/Da / Density % sol: 60.93 % |
---|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
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
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.7→8 Å / σ(F): 1
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|