+
Open data
-
Basic information
Entry | Database: PDB / ID: 2gr9 | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of P5CR complexed with NADH | ||||||
![]() | Pyrroline-5-carboxylate reductase 1 | ||||||
![]() | OXIDOREDUCTASE / crystal strucutre / Human Pyrroline-5-carboxylate Reductase / nadh | ||||||
Function / homology | ![]() pyrroline-5-carboxylate reductase / pyrroline-5-carboxylate reductase activity / L-proline biosynthetic process / Glutamate and glutamine metabolism / proline biosynthetic process / negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway / regulation of mitochondrial membrane potential / cellular response to oxidative stress / mitochondrial matrix / mitochondrion / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Meng, Z. / Lou, Z. / Liu, Z. / Rao, Z. | ||||||
![]() | ![]() Title: Crystal structure of human pyrroline-5-carboxylate reductase Authors: Meng, Z. / Lou, Z. / Liu, Z. / Li, M. / Zhao, X. / Bartlam, M. / Rao, Z. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 287.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 229.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.4 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 2.6 MB | Display | |
Data in XML | ![]() | 103.3 KB | Display | |
Data in CIF | ![]() | 132.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2gerSC ![]() 2graC C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
3 | ![]()
| ||||||||
4 | ![]()
| ||||||||
5 | ![]()
| ||||||||
6 | ![]()
| ||||||||
7 | ![]()
| ||||||||
8 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 29147.648 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P32322, pyrroline-5-carboxylate reductase #2: Chemical | ChemComp-NAI / #3: Chemical | ChemComp-GLU / #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 4.48 Å3/Da / Density % sol: 72.55 % |
---|---|
Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 0.8-1M sodium acetate, 30-40mM imidazole (pH 6.5), 50-60mM Tris-HCl (pH 7.5), VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 17, 2005 |
Radiation | Monochromator: osmic mirror / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→50 Å / Num. all: 159528 / Num. obs: 158126 / % possible obs: 99 % / Observed criterion σ(F): 0 |
Reflection shell | Resolution: 3.1→3.2 Å / % possible all: 99 |
-
Processing
Software |
| |||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 2GER Resolution: 3.1→50 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
| |||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→50 Å
| |||||||||||||||||||||
Refine LS restraints |
|