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- PDB-2acu: TYROSINE-48 IS THE PROTON DONOR AND HISTIDINE-110 DIRECTS SUBSTRA... -
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Open data
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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 | ||||||
![]() | ALDOSE REDUCTASE![]() | ||||||
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Function / homology | ![]() glyceraldehyde oxidoreductase activity / Fructose biosynthesis / fructose biosynthetic process / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Bohren, K.M. / Grimshaw, C.E. / Lai, C.-J. / Gabbay, K.H. / Petsko, G.A. / Harrison, D.H. / Ringe, D. | ||||||
![]() | ![]() 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: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.4 KB | Display | ![]() |
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PDB format | ![]() | 59 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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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. |
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Components
#1: Protein | ![]() Mass: 35742.121 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-NAP / ![]() |
#3: Chemical | ChemComp-CIT / ![]() |
#4: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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 % |
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Processing
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Refinement | Rfactor Rwork![]() | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.76 Å
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Software | *PLUS Name: ![]() | ||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å / σ(I): 1 / Rfactor obs: 0.187 / Rfactor Rwork![]() | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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