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- PDB-2h1v: Crystal structure of the Lys87Ala mutant variant of Bacillus subt... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2h1v | ||||||
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Title | Crystal structure of the Lys87Ala mutant variant of Bacillus subtilis ferrochelatase | ||||||
![]() | Ferrochelatase | ||||||
![]() | LYASE / ROSSMANN FOLD / PI-HELIX | ||||||
Function / homology | ![]() coproporphyrin ferrochelatase / ferrochelatase activity / heme biosynthetic process / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hansson, M.D. / Karlberg, T. / Arys Rahardja, M. / Al-Karadaghi, S. / Hansson, M. | ||||||
![]() | ![]() Title: Amino Acid Residues His183 and Glu264 in Bacillus subtilis Ferrochelatase Direct and Facilitate the Insertion of Metal Ion into Protoporphyrin IX Authors: Hansson, M.D. / Karlberg, T. / Rahardja, M.A. / Al-Karadaghi, S. / Hansson, M. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 162.4 KB | Display | ![]() |
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PDB format | ![]() | 126.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2h1wC ![]() 2hk6C ![]() 1dozS 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: 35331.602 Da / Num. of mol.: 1 / Mutation: K87A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
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#2: Chemical | ChemComp-MG / #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.95 Å3/Da / Density % sol: 37.02 % |
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Crystal grow | Temperature: 288 K / Method: vapor diffusion / pH: 7.4 Details: 25-30% PEG 2000, 0.2 M magnesium chloride, 0.1 M Tris-HCl, pH 7.4, VAPOR DIFFUSION, temperature 288K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 18, 2004 |
Radiation | Monochromator: Bent germanium crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.043 Å / Relative weight: 1 |
Reflection | Resolution: 1.2→25 Å / Num. all: 83335 / Num. obs: 83273 / % possible obs: 93.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 5.1 % / Rmerge(I) obs: 0.067 / Net I/σ(I): 14 |
Reflection shell | Resolution: 1.2→1.27 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.233 / Mean I/σ(I) obs: 5 / Num. unique all: 9813 / % possible all: 70.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1DOZ Resolution: 1.2→25 Å / Num. parameters: 27732 / Num. restraintsaints: 34600 / Isotropic thermal model: anisotropic / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER Details: ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY 0.034
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Refine analyze | Num. disordered residues: 12 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 2971.5 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.2→25 Å
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Refine LS restraints |
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