[English] 日本語
Yorodumi- PDB-1mar: REFINED 1.8 ANGSTROMS STRUCTURE OF HUMAN ALDOSE REDUCTASE COMPLEX... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1mar | ||||||
---|---|---|---|---|---|---|---|
Title | REFINED 1.8 ANGSTROMS STRUCTURE OF HUMAN ALDOSE REDUCTASE COMPLEXED WITH THE POTENT INHIBITOR ZOPOLRESTAT | ||||||
Components | ALDOSE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE(NADP) | ||||||
Function / homology | Function and homology information glyceraldehyde oxidoreductase activity / Fructose biosynthesis / fructose biosynthetic process / L-glucuronate reductase activity / glycerol dehydrogenase (NADP+) activity / D/L-glyceraldehyde reductase / aldose reductase / C21-steroid hormone biosynthetic process / Pregnenolone biosynthesis / NADP-retinol dehydrogenase ...glyceraldehyde oxidoreductase activity / Fructose biosynthesis / fructose biosynthetic process / L-glucuronate reductase activity / glycerol dehydrogenase (NADP+) activity / D/L-glyceraldehyde reductase / aldose reductase / C21-steroid hormone biosynthetic process / Pregnenolone biosynthesis / NADP-retinol dehydrogenase / allyl-alcohol dehydrogenase / allyl-alcohol dehydrogenase activity / L-ascorbic acid biosynthetic process / metanephric collecting duct development / prostaglandin H2 endoperoxidase reductase activity / regulation of urine volume / all-trans-retinol dehydrogenase (NADP+) activity / renal water homeostasis / daunorubicin metabolic process / doxorubicin metabolic process / epithelial cell maturation / retinal dehydrogenase activity / aldose reductase (NADPH) activity / retinoid metabolic process / cellular hyperosmotic salinity response / carbohydrate metabolic process / electron transfer activity / negative regulation of apoptotic process / extracellular space / extracellular exosome / nucleoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | ||||||
Authors | Wilson, D.K. / Quiocho, F.A. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1993 Title: Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Authors: Wilson, D.K. / Tarle, I. / Petrash, J.M. / Quiocho, F.A. #1: Journal: Science / Year: 1992 Title: An Unlikely Sugar Substrate Site in the 1.65 Angstroms Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications Authors: Wilson, D.K. / Bohren, K.M. / Gabbay, K.H. / Quiocho, F.A. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1mar.cif.gz | 25 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1mar.ent.gz | 12.8 KB | Display | PDB format |
PDBx/mmJSON format | 1mar.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mar_validation.pdf.gz | 441.6 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1mar_full_validation.pdf.gz | 442 KB | Display | |
Data in XML | 1mar_validation.xml.gz | 1.6 KB | Display | |
Data in CIF | 1mar_validation.cif.gz | 4.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ma/1mar ftp://data.pdbj.org/pub/pdb/validation_reports/ma/1mar | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 35767.145 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P15121, aldose reductase |
---|---|
#2: Chemical | ChemComp-NAP / |
#3: Chemical | ChemComp-ZST / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.19 % | ||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 20 Å / Num. obs: 26145 / % possible obs: 90.4 % / Num. measured all: 53037 / Rmerge(I) obs: 0.034 |
---|
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.8→12 Å / σ(F): 1 /
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→12 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.18 / Rfactor Rwork: 0.18 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |