[English] 日本語
![](img/lk-miru.gif)
- PDB-2vzl: FERREDOXIN-NADP REDUCTASE (MUTATIONS: T155G, A160T, L263P AND Y30... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2vzl | ||||||
---|---|---|---|---|---|---|---|
Title | FERREDOXIN-NADP REDUCTASE (MUTATIONS: T155G, A160T, L263P AND Y303S) COMPLEXED WITH NAD BY COCRYSTALLIZATION | ||||||
![]() | FERREDOXIN-NADP REDUCTASE![]() | ||||||
![]() | ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Herguedas, B. / Martinez-Julvez, M. / Hermoso, J.A. / Peregrina, J.R. / Medina, M. | ||||||
![]() | ![]() Title: Protein Motifs Involved in Coenzyme Interaction and Enzymatic Efficiency in Anabaena Ferredoxin-Nadp+ Reductase. Authors: Peregrina, J.R. / Herguedas, B. / Hermoso, J.A. / Martinez-Julvez, M. / Medina, M. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 87.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 63.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 2bmwC ![]() 2vyqC ![]() 1queS C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | ![]() Mass: 34067.691 Da / Num. of mol.: 1 / Fragment: RESIDUES 137-440 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
---|---|
#2: Chemical | ChemComp-FAD / ![]() |
#3: Chemical | ChemComp-NAD / ![]() |
#4: Chemical | ChemComp-GOL / ![]() |
#5: Water | ChemComp-HOH / ![]() |
Compound details | ENGINEERED RESIDUE IN CHAIN A, THR 292 TO GLY ENGINEERED RESIDUE IN CHAIN A, ALA 297 TO THR ...ENGINEERED |
Nonpolymer details | NICOTINAMIDE-ADENINE-DINUCLEOTIDE (NAD): ONLY ADP MOEITY IS OBSERVED TWO ALTERNATE CONFORMATIONS ...NICOTINAMI |
Sequence details | FNR MUTANT (T155G, A160T, L263P, Y303S) |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.92 Å3/Da / Density % sol: 57.8 % / Description: NONE |
---|---|
Crystal grow![]() | pH: 5.5 Details: 20% PEG 6000 0.1M ACNA, PH 5.5 B-OCTYL GLYCOSIDE AT 2%(W/V) 10-60 MM NAD |
-Data collection
Diffraction | Mean temperature: 120 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: BRUKER-NONIUS / Detector: CCD / Date: Dec 12, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.93→43.44 Å / Num. obs: 31094 / % possible obs: 100 % / Observed criterion σ(I): 2 / Redundancy: 8.4 % / Rmerge(I) obs: 0.12 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 1.93→2 Å / Redundancy: 5.9 % / Rmerge(I) obs: 0.47 / % possible all: 99.7 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1QUE Resolution: 1.93→20 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.919 / SU B: 2.605 / SU ML: 0.076 / Cross valid method: THROUGHOUT / ESU R: 0.135 / ESU R Free: 0.121 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 11.56 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.93→20 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|