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Yorodumi- PDB-2acu: TYROSINE-48 IS THE PROTON DONOR AND HISTIDINE-110 DIRECTS SUBSTRA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2acu | ||||||
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Title | TYROSINE-48 IS THE PROTON DONOR AND HISTIDINE-110 DIRECTS SUBSTRATE STEREOCHEMICAL SELECTIVITY IN THE REDUCTION REACTION OF HUMAN ALDOSE REDUCTASE: ENZYME KINETICS AND THE CRYSTAL STRUCTURE OF THE Y48H MUTANT ENZYME | ||||||
Components | ALDOSE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE | ||||||
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 / L-ascorbic acid biosynthetic process / allyl-alcohol dehydrogenase / allyl-alcohol dehydrogenase activity / metanephric collecting duct development / prostaglandin H2 endoperoxidase reductase activity / regulation of urine volume / all-trans-retinol dehydrogenase (NADP+) activity / renal water homeostasis / epithelial cell maturation / daunorubicin metabolic process / doxorubicin metabolic process / retinal dehydrogenase activity / aldose reductase (NADPH) activity / retinoid metabolic process / cellular hyperosmotic salinity response / electron transfer activity / carbohydrate metabolic process / negative regulation of apoptotic process / extracellular space / extracellular exosome / nucleoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.76 Å | ||||||
Authors | Bohren, K.M. / Grimshaw, C.E. / Lai, C.-J. / Gabbay, K.H. / Petsko, G.A. / Harrison, D.H. / Ringe, D. | ||||||
Citation | Journal: Biochemistry / Year: 1994 Title: Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme. Authors: Bohren, K.M. / Grimshaw, C.E. / Lai, C.J. / Harrison, D.H. / Ringe, D. / Petsko, G.A. / Gabbay, K.H. #1: Journal: Biochemistry / Year: 1994 Title: An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications for the Binding of Citrate, Cacodylate, and Glucose-6-Phosphate Authors: Harrison, D.H. / Bohren, K.M. / Ringe, D. / Petsko, G.A. / Gabbay, K.H. #2: 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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2acu.cif.gz | 78.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2acu.ent.gz | 59 KB | Display | PDB format |
PDBx/mmJSON format | 2acu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ac/2acu ftp://data.pdbj.org/pub/pdb/validation_reports/ac/2acu | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUE 316 (NAP) IS THE NADP+ COFACTOR. / 2: RESIDUE 317 (CIT) IS THE BOUND CITRATE ION. |
-Components
#1: Protein | Mass: 35742.121 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 |
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#2: Chemical | ChemComp-NAP / |
#3: Chemical | ChemComp-CIT / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.06 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / pH: 5 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.76 Å / Lowest resolution: 9999 Å / Num. obs: 23622 / Observed criterion σ(I): 0 / Num. measured all: 75201 / Rmerge(I) obs: 0.117 |
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Reflection shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 2 Å / % possible obs: 40.8 % |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.187 / Rfactor obs: 0.187 / Highest resolution: 1.76 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.76 Å
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å / σ(I): 1 / Rfactor obs: 0.187 / Rfactor Rwork: 0.187 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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