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Open data
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Basic information
Entry | Database: PDB / ID: 1b2j | ||||||
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Title | CLOSTRIDIUM PASTEURIANUM RUBREDOXIN G43A MUTANT | ||||||
![]() | PROTEIN (RUBREDOXIN) | ||||||
![]() | ELECTRON TRANSPORT / METALLOPROTEIN / IRON SULFUR / ELECTRON TRANSFER | ||||||
Function / homology | ![]() alkane catabolic process / electron transfer activity / iron ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Maher, M.J. / Guss, J.M. / Wilce, M.C.J. / Wedd, A.G. | ||||||
![]() | ![]() Title: Rubredoxin from Clostridium pasteurianum. Structures of G10A, G43A and G10VG43A mutant proteins. Mutation of conserved glycine 10 to valine causes the 9-10 peptide link to invert. Authors: Maher, M.J. / Xiao, Z. / Wilce, M.C. / Guss, J.M. / Wedd, A.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 23 KB | Display | ![]() |
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PDB format | ![]() | 14 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1b13C ![]() 1b2oC ![]() 5rxnS S: Starting model for refinement 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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Unit cell |
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Components
#1: Protein | Mass: 6065.637 Da / Num. of mol.: 1 / Mutation: G43A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-FE / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.2 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 4.6 Details: PROTEIN WAS CRYSTALLISED FROM 50-60% SATURATED AMMONIUM SULFATE IN SODIUM ACETATE BUFFER (50 MM) AT PH 4.5., pH 4.6 | ||||||||||||||||||||||||||||||
Components of the solutions |
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Crystal | *PLUS | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 277 K / Method: vapor diffusion, hanging drop / PH range low: 5 / PH range high: 4 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RU200 / Detector: IMAGE PLATE / Date: May 1, 1996 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER 0.00015" / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→30 Å / Num. obs: 6484 / % possible obs: 97.2 % / Redundancy: 2 % / Rmerge(I) obs: 0.067 / Net I/σ(I): 9.5 |
Reflection shell | Resolution: 1.6→1.66 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.217 / Mean I/σ(I) obs: 3.2 / % possible all: 86 |
Reflection | *PLUS Num. measured all: 17201 |
Reflection shell | *PLUS % possible obs: 86 % |
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Processing
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Refinement | Method to determine structure: OTHER Starting model: 5RXN Resolution: 1.6→30 Å / σ(F): 0 / Details: ESD FROM CRUIKSHANK (A): 0.09
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Displacement parameters | Biso mean: 23 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→30 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.6 Å / % reflection Rfree: 5 % / Rfactor obs: 0.182 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 23 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.364 / Rfactor obs: 0.282 |