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- PDB-1zk3: Triclinic crystal structure of the apo-form of R-specific alcohol... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1zk3 | ||||||
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Title | Triclinic crystal structure of the apo-form of R-specific alcohol dehydrogenase (mutant G37D) from Lactobacillus brevis | ||||||
![]() | R-specific alcohol dehydrogenase | ||||||
![]() | OXIDOREDUCTASE / short chain reductases/dehydrogenases / magnesium dependence / R-specific alcohol dehydrogenase | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Schlieben, N.H. / Niefind, K. / Muller, J. / Riebel, B. / Hummel, W. / Schomburg, D. | ||||||
![]() | ![]() Title: Atomic Resolution Structures of R-specific Alcohol Dehydrogenase from Lactobacillus brevis Provide the Structural Bases of its Substrate and Cosubstrate Specificity Authors: Schlieben, N.H. / Niefind, K. / Muller, J. / Riebel, B. / Hummel, W. / Schomburg, D. #1: ![]() Title: The crystal structure of R-specific alcohol dehydrogenase from Lactobacillus brevis suggests the structural basis of its metal dependency Authors: Niefind, K. / Muller, J. / Riebel, B. / Hummel, W. / Schomburg, D. #2: Journal: Acta Crystallogr.,Sect.D / Year: 2000 Title: Crystallization and preliminary characterization of crystals of R-alcohol dehydrogenase from Lactobacills brevis Authors: Niefind, K. / Riebel, B. / Muller, J. / Hummel, W. / Schomburg, D. | ||||||
History |
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Remark 600 | HETEROGEN Water molecules 253-375 are associated with chain A, 453-575 are associated with chain ... HETEROGEN Water molecules 253-375 are associated with chain A, 453-575 are associated with chain B, 653-775 are associated with chain C, 853-975 are associated with chain D, 1053-1175 are associated with chain E, 1253-1375 are associated with chain F, 1453-1575 are associated with chain G and 1653-1775 are associated with chain H. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 390.5 KB | Display | ![]() |
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PDB format | ![]() | 319.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 471.2 KB | Display | ![]() |
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Full document | ![]() | 495.6 KB | Display | |
Data in XML | ![]() | 81.6 KB | Display | |
Data in CIF | ![]() | 114.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1zjyC ![]() 1zjzC ![]() 1zk0C ![]() 1zk1C ![]() 1zk2C ![]() 1zk4C C: citing same article ( |
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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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Details | The biological assembly is a tetramer. The asymmetric unit contains eight monomers belonging to two different tetramers.The chains A, B, C, and D form one tetramer and the chains E, F, G, and H the other. |
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Components
#1: Protein | Mass: 26714.098 Da / Num. of mol.: 8 / Mutation: G37D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-MG / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 44.8 % |
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-Data collection
Diffraction source | Source: ![]() |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→63.8 Å / Num. all: 94706 / Num. obs: 94706 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.2→63.8 Å
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Xplor file |
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