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- PDB-2po5: Crystal structure of human ferrochelatase mutant with His 263 rep... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2po5 | ||||||
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Title | Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys | ||||||
![]() | Ferrochelatase, mitochondrial![]() | ||||||
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Function / homology | ![]() protoporphyrinogen IX metabolic process / regulation of hemoglobin biosynthetic process / regulation of eIF2 alpha phosphorylation by heme / detection of UV / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Dailey, H.A. / Wu, C.-K. / Horanyi, P. / Medlock, A.E. / Najahi-Missaoui, A.E.W. / Burden, A. / Dailey, T.A. / Rose, J.P. | ||||||
![]() | ![]() Title: Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis Authors: Dailey, H.A. / Wu, C.-K. / Horanyi, P. / Medlock, A.E. / Najahi-Missaoui, W. / Burden, A.E. / Dailey, T.A. / Rose, J.P. #1: ![]() Title: The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis Authors: Wu, C.K. / Dailey, H.A. / Rose, J.P. / Burden, A. / Sellers, V.M. / Wang, B.-C. #2: Journal: Biochim.Biophys.Acta / Year: 1999 Title: Human Ferrochelatase: Crystallization, Characterization of the [2Fe-2S] Cluster and Determination that the Enzyme is a Homodimer Authors: Burden, A.E. / Wu, C.-K. / Dailey, T.A. / Busch, J.L.H. / Dhawan, I.K. / Rose, J.P. / Wang, B.C. / Dailey, H.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 | ![]() | 164.2 KB | Display | ![]() |
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PDB format | ![]() | 128.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 41099.344 Da / Num. of mol.: 2 / Fragment: Mature Protein / Mutation: R115L, H263C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Chemical | ![]() #3: Chemical | ChemComp-CHD / ![]() #4: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.73 Å3/Da / Density % sol: 54.94 % |
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Crystal grow![]() | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: CRYSTALS WERE GROWN BY HANGING DROP VAPOR DIFFUSION USING 2 MICROLITER DROPS CONTAINING EQUAL VOLUMES OF PROTEIN SOLUTION (50 MG/ML IN 50 MM TRIS MOPS, 0.1M KCL, 1% NA- CHOLATE, 250 MM ...Details: CRYSTALS WERE GROWN BY HANGING DROP VAPOR DIFFUSION USING 2 MICROLITER DROPS CONTAINING EQUAL VOLUMES OF PROTEIN SOLUTION (50 MG/ML IN 50 MM TRIS MOPS, 0.1M KCL, 1% NA- CHOLATE, 250 MM IMIDAZOLE, PH 8.1) AND PRECIPITANT SOLUTION (0.1 M HEPES PH 7.5, 0.2 M AMMONIUM SULFATE, 34% PEG 400, 0.1 M SODIUM PHOSPHATE)., pH 7.50, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 25, 2001 / Details: RIGAKU BLUE CONFOCAL |
Radiation | Monochromator: RIGAKU BLUE CONFOCAL Optics / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2→50 Å / Num. all: 45450 / Num. obs: 45450 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.065 |
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Processing
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Refinement | Method to determine structure![]()
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 36.33 Å2 / ksol: 0.38 e/Å3 | |||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.2→19.9 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.34 Å / Rfactor Rfree: 0.272 / Rfactor Rwork: 0.242 / Total num. of bins used: 2 | |||||||||||||||||||||||||
Xplor file |
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