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- PDB-1yve: ACETOHYDROXY ACID ISOMEROREDUCTASE COMPLEXED WITH NADPH, MAGNESIU... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1yve | ||||||
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Title | ACETOHYDROXY ACID ISOMEROREDUCTASE COMPLEXED WITH NADPH, MAGNESIUM AND INHIBITOR IPOHA (N-HYDROXY-N-ISOPROPYLOXAMATE) | ||||||
![]() | ACETOHYDROXY ACID ISOMEROREDUCTASE | ||||||
![]() | OXIDOREDUCTASE / BRANCHED-CHAIN AMINO ACID BIOSYNTHESIS / MAGNESIUM / NADP / CHLOROPLAST / TRANSIT PEPTIDE | ||||||
Function / homology | ![]() ketol-acid reductoisomerase (NADP+) / ketol-acid reductoisomerase activity / valine biosynthetic process / isoleucine biosynthetic process / NADPH binding / amino acid biosynthetic process / chloroplast / magnesium ion binding / protein homodimerization activity / mitochondrion / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Biou, V. / Dumas, R. / Cohen-Addad, C. / Douce, R. / Job, D. / Pebay-Peyroula, E. | ||||||
![]() | ![]() Title: The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution. Authors: Biou, V. / Dumas, R. / Cohen-Addad, C. / Douce, R. / Job, D. / Pebay-Peyroula, E. #1: ![]() Title: Crystallization and Preliminary Crystallographic Data for Acetohydroxy Acid Isomeroreductase from Spinacia Oleracea Authors: Dumas, R. / Job, D. / Douce, R. / Pebay-Peyroula, E. / Cohen-Addad, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 440.2 KB | Display | ![]() |
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PDB format | ![]() | 355.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 699.2 KB | Display | ![]() |
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Full document | ![]() | 722 KB | Display | |
Data in XML | ![]() | 41.9 KB | Display | |
Data in CIF | ![]() | 72.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
-Protein , 1 types, 4 molecules IJKL
#1: Protein | Mass: 57045.543 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene (production host): CDNA FROM ACETOHYDROXY ACID ISOMEROREDUCTASE Production host: ![]() ![]() References: UniProt: Q01292, ketol-acid reductoisomerase (NADP+) |
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-Non-polymers , 5 types, 1808 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/NDP.gif)
![](data/chem/img/HIO.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/NDP.gif)
![](data/chem/img/HIO.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-MG / #3: Chemical | #4: Chemical | ChemComp-NDP / #5: Chemical | ChemComp-HIO / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.45 Å3/Da / Density % sol: 54 % Description: TEMPERATURE OF DATA COLLECTION : 100K CRYSTAL WAS FLASH FROZEN IN 20% GLYCEROL/MOTHER LIQUOR SOLUTION. | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.2 / Method: unknown | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 12, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95 Å / Relative weight: 1 |
Reflection | Num. obs: 242843 / % possible obs: 92 % / Observed criterion σ(I): 0 / Redundancy: 3.99 % / Rmerge(I) obs: 0.064 |
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Processing
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Refinement | Resolution: 1.65→10 Å / σ(F): 0
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Displacement parameters | Biso mean: 18.2 Å2
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Refinement step | Cycle: LAST / Resolution: 1.65→10 Å
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Xplor file |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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