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Open data
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Basic information
Entry | Database: PDB / ID: 1qcw | ||||||
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Title | Flavocytochrome B2, ARG289LYS mutant | ||||||
![]() | FLAVOCYTOCHROME B2 | ||||||
![]() | OXIDOREDUCTASE / FLAVOPROTEIN ELECTRON TRANSFER MUTAGENISIS | ||||||
Function / homology | ![]() L-lactate dehydrogenase (cytochrome) / L-lactate dehydrogenase (cytochrome) activity / lactate metabolic process / : / mitochondrial intermembrane space / mitochondrial inner membrane / heme binding / mitochondrion / nucleus / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Mowat, C.G. / Durley, R.C.E. / Pike, A.D. / Barton, J.D. / Chen, Z.-W. / Mathews, F.S. / Lederer, F. / Reid, G.A. / Chapman, S.K. | ||||||
![]() | ![]() Title: Kinetic and crystallographic studies on the active site Arg289Lys mutant of flavocytochrome b2 (yeast L-lactate dehydrogenase) Authors: Mowat, C.G. / Beaudoin, I. / Durley, R.C.E. / Barton, J.D. / Pike, A.D. / Chen, Z.-W. / Reid, G.A. / Chapman, S.K. / Mathews, F.S. / Lederer, F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 161.9 KB | Display | ![]() |
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PDB format | ![]() | 128.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 537.3 KB | Display | ![]() |
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Full document | ![]() | 558.1 KB | Display | |
Data in XML | ![]() | 18.9 KB | Display | |
Data in CIF | ![]() | 27.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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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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Unit cell |
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Components
#1: Protein | Mass: 45527.176 Da / Num. of mol.: 2 / Mutation: R289K, P304F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() References: UniProt: P00175, L-lactate dehydrogenase (cytochrome) #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.69 Å3/Da / Density % sol: 73.78 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 288 K / Method: vapor diffusion, sitting drop / pH: 7 Details: pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 288K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Mar 31, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.75→30 Å / Num. all: 36062 / % possible obs: 80.8 % / Redundancy: 1.7 % / Rmerge(I) obs: 0.078 / Net I/σ(I): 7.8 |
Reflection shell | Resolution: 2.75→2.87 Å / Redundancy: 1.3 % / Rmerge(I) obs: 0.416 / Num. unique all: 36062 / % possible all: 75.2 |
Reflection | *PLUS Num. obs: 36062 |
Reflection shell | *PLUS % possible obs: 75.2 % / Mean I/σ(I) obs: 1.3 |
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Processing
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Refinement | Resolution: 2.75→8 Å / σ(I): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.75→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | |||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 500 Å / Rfactor Rfree: 0.221 / Rfactor Rwork: 0.207 | |||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 2.75 Å / Lowest resolution: 2.88 Å / Rfactor Rfree: 0.338 / Rfactor Rwork: 0.299 |