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- PDB-1mra: MANDELATE RACEMASE MUTANT D270N CO-CRYSTALLIZED WITH (S)-ATROLACTATE -
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Open data
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Basic information
Entry | Database: PDB / ID: 1mra | ||||||
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Title | MANDELATE RACEMASE MUTANT D270N CO-CRYSTALLIZED WITH (S)-ATROLACTATE | ||||||
![]() | MANDELATE RACEMASE | ||||||
![]() | RACEMASE / ISOMERASE / MANDELATE PATHWAY / ATROLACTATE / MAGNESIUM RACEMASE | ||||||
Function / homology | ![]() mandelate racemase / mandelate racemase activity / mandelate catabolic process / amino acid catabolic process / hydro-lyase activity / carbohydrate catabolic process / magnesium ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Clifton, J.G. / Petsko, G.A. | ||||||
![]() | ![]() Title: Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant. Authors: Schafer, S.L. / Barrett, W.C. / Kallarakal, A.T. / Mitra, B. / Kozarich, J.W. / Gerlt, J.A. / Clifton, J.G. / Petsko, G.A. / Kenyon, G.L. #1: ![]() Title: Mechanism of the Reaction Catalyzed by Mandelate Racemase. 2. Crystal Structure of Mandelate Racemase at 2.5-A Resolution: Identification of the Active Site and Possible Catalytic Residues Authors: Neidhart, D.J. / Howell, P.L. / Petsko, G.A. / Powers, V.M. / Li, R.S. / Kenyon, G.L. / Gerlt, J.A. #2: ![]() Title: Mandelate Racemase and Muconate Lactonizing Enzyme are Mechanistically Distinct and Structurally Homologous Authors: Neidhart, D.J. / Kenyon, G.L. / Gerlt, J.A. / Petsko, G.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 | ![]() | 83.3 KB | Display | ![]() |
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PDB format | ![]() | 61.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 384.4 KB | Display | ![]() |
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Full document | ![]() | 399.6 KB | Display | |
Data in XML | ![]() | 10.4 KB | Display | |
Data in CIF | ![]() | 15.5 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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Unit cell |
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Components
#1: Protein | Mass: 38601.613 Da / Num. of mol.: 1 / Mutation: D270N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-APG / |
#4: Water | ChemComp-HOH / |
Nonpolymer details | THIS IS THE STRUCTURE OF THE MANDELATE RACEMASE MUTANT ASPARTATE 270 -> ASPARAGINE CO-CRYSTALLIZED ...THIS IS THE STRUCTURE OF THE MANDELATE RACEMASE MUTANT ASPARTATE 270 -> ASPARAGINE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 55 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Details: THE INHIBITOR CONSTANT (K SUB I) FOR (S)-ATROLACTATE IS APPROXIMATELY 0.2 MILLIMOLAR; CRYSTALS WERE OBTAINED FROM A SOLUTION THAT CONTAINED 5 MILLIMOLAR INHIBITOR. | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging drop / Details: Mitra, B., (1995) Biochemistry, 34, 2777. | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Jul 25, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 24713 / % possible obs: 74.6 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.171 / Net I/σ(I): 1 |
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Processing
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Refinement | Resolution: 2.1→20 Å / Isotropic thermal model: TNT / σ(F): 1 / Stereochemistry target values: TNT Details: RESIDUES LEU 18 - THR 31: THE ELECTRON DENSITY FOR THE RESIDUES IN THE "FLAP" REGION CONTAINED MULTIPLE BREAKS. IT IS LIKELY THAT THE "FLAP" RESIDUES WERE ACTUALLY PRESENT IN MULTIPLE ...Details: RESIDUES LEU 18 - THR 31: THE ELECTRON DENSITY FOR THE RESIDUES IN THE "FLAP" REGION CONTAINED MULTIPLE BREAKS. IT IS LIKELY THAT THE "FLAP" RESIDUES WERE ACTUALLY PRESENT IN MULTIPLE CONFORMATIONS. HOWEVER, THEY WERE REFINED IN THESE CONFORMATIONS WITH THEIR OCCUPANCIES SET TO 1.0. CONSEQUENTLY, THEIR B-FACTORS ARE GREATER THAN THE REST OF THE PROTEIN. FURTHERMORE, THE LACK OF "ENCLOSING" ELECTRON DENSITY CAUSED MORE SIGNIFICANT GEOMETRIC DEVIATIONS DURING REFINEMENT.
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Refinement step | Cycle: LAST / Resolution: 2.1→20 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.19 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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