[English] 日本語
![](img/lk-miru.gif)
- PDB-2vne: The X-ray structure of Norcoclaurine synthase from Thalictrum flavum -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2vne | ||||||
---|---|---|---|---|---|---|---|
Title | The X-ray structure of Norcoclaurine synthase from Thalictrum flavum | ||||||
![]() | S-NORCOCLAURINE SYNTHASE | ||||||
![]() | LYASE / NORCOCLAURINE SYNTHASE / BIOSYNTHESIS OF BENZYLISOQUINOLINE ALKALOIDS | ||||||
Function / homology | ![]() (S)-norcoclaurine synthase / (S)-norcoclaurine synthase activity / alkaloid metabolic process / abscisic acid binding / abscisic acid-activated signaling pathway / protein phosphatase inhibitor activity / defense response / signaling receptor activity / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ilari, A. / Franceschini, S. / Boffi, A. / Bonamore, A. / Pasquo, A. | ||||||
![]() | ![]() Title: Structural Basis of Enzymatic S-Norcoclaurine Biosynthesis. Authors: Ilari, A. / Franceschini, S. / Bonamore, A. / Arenghi, F. / Botta, B. / Macone, A. / Pasquo, A. / Bellucci, L. / Boffi, A. #1: Journal: Acta Crystallogr.,Sect.F / Year: 2008 Title: Cloning, Expression, Crystallization and Preliminary X-Ray Data Analysis of Norcoclaurine Synthase from Thalictrum Flavum. Authors: Pasquo, A. / Bonamore, A. / Franceschini, S. / Macone, A. / Boffi, A. / Ilari, A. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 72.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 58.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 441.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 448 KB | Display | |
Data in XML | ![]() | 13.7 KB | Display | |
Data in CIF | ![]() | 18 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 22606.209 Da / Num. of mol.: 2 / Fragment: RESIDUES 16-210 / Mutation: YES Source method: isolated from a genetically manipulated source Details: THE PROTEIN LACKS THE FIRST 15 RESIDUES AND IS HIS-TAGGED AT THE C-TERMINUS. Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, THR 16 TO MSE ENGINEERED RESIDUE IN CHAIN A, ILE 17 TO THR ...ENGINEERED | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.52 Å3/Da / Density % sol: 64.83 % / Description: NONE |
---|---|
Crystal grow | pH: 4.5 Details: AMMONIUM SULPHATE 0.8-1.3 M, SODIUM CHLORIDE 0.1-0.3 M, ACETATE BUFFER 0.1 M AT PH=4.5 . |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 28, 2007 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.978 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. obs: 13618 / % possible obs: 96 % / Redundancy: 4.6 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 14 |
Reflection shell | Resolution: 2.7→2.8 Å / Redundancy: 4 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 2 / % possible all: 94.1 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 2.72→74.74 Å / Cor.coef. Fo:Fc: 0.923 / Cor.coef. Fo:Fc free: 0.891 / SU B: 13.867 / SU ML: 0.282 / Cross valid method: THROUGHOUT / ESU R: 0.674 / ESU R Free: 0.358 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 58.71 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.72→74.74 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|