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Yorodumi- PDB-2po7: Crystal structure of human ferrochelatase mutant with His 341 rep... -
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-Basic information
Entry | Database: PDB / ID: 2po7 | ||||||
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Title | Crystal structure of human ferrochelatase mutant with His 341 replaced by Cys | ||||||
Components | Ferrochelatase, mitochondrial | ||||||
Keywords | LYASE / FERROCHELATASE / H341C / FE2S2 CLUSTER / HEME BIOSYNTHESIS / PROTOHEME / FERRO-LYASE / MATURE LENGTH / PROTEOLYTICALLY PROCESSED MITOCHONDRIAL INNER MEMBRANE PROTEIN | ||||||
Function / homology | Function and homology information protoporphyrinogen IX metabolic process / regulation of hemoglobin biosynthetic process / regulation of eIF2 alpha phosphorylation by heme / detection of UV / iron-responsive element binding / response to platinum ion / protoporphyrin ferrochelatase / response to insecticide / heme B biosynthetic process / heme O biosynthetic process ...protoporphyrinogen IX metabolic process / regulation of hemoglobin biosynthetic process / regulation of eIF2 alpha phosphorylation by heme / detection of UV / iron-responsive element binding / response to platinum ion / protoporphyrin ferrochelatase / response to insecticide / heme B biosynthetic process / heme O biosynthetic process / ferrochelatase activity / heme A biosynthetic process / very-low-density lipoprotein particle assembly / response to methylmercury / response to arsenic-containing substance / Heme biosynthesis / heme biosynthetic process / response to light stimulus / cholesterol metabolic process / erythrocyte differentiation / cellular response to dexamethasone stimulus / generation of precursor metabolites and energy / response to lead ion / ferrous iron binding / 2 iron, 2 sulfur cluster binding / multicellular organismal-level iron ion homeostasis / response to ethanol / mitochondrial inner membrane / mitochondrial matrix / response to xenobiotic stimulus / heme binding / protein homodimerization activity / mitochondrion / identical protein binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / DIFFERENCE FOURIER / Resolution: 2.2 Å | ||||||
Authors | Dailey, H.A. / Wu, C.-K. / Horanyi, P. / Medlock, A.E. / Najahi-Missaoui, W. / Burden, A. / Dailey, T.A. / Rose, J.P. | ||||||
Citation | Journal: Biochemistry / Year: 2007 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. #1: Journal: Nat.Struct.Biol. / Year: 2001 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2po7.cif.gz | 167.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2po7.ent.gz | 130.3 KB | Display | PDB format |
PDBx/mmJSON format | 2po7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/po/2po7 ftp://data.pdbj.org/pub/pdb/validation_reports/po/2po7 | HTTPS FTP |
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-Related structure data
Related structure data | 2pnjC 2po5C 1hrkS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 41070.281 Da / Num. of mol.: 2 / Fragment: Mature Protein / Mutation: R115L, H341C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FECH / Plasmid: PHDTF20 / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: P22830, protoporphyrin ferrochelatase #2: Chemical | #3: Chemical | ChemComp-CHD / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.77 Å3/Da / Density % sol: 55.64 % |
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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 (45 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 (45 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: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 20, 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: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→50 Å / Num. obs: 41766 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.068 |
-Processing
Software |
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: 1HRK Resolution: 2.2→18.08 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 49.2589 Å2 / ksol: 0.4335 e/Å3 | |||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.2→18.08 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.34 Å / Rfactor Rfree: 0.29 / Rfactor Rwork: 0.222 | |||||||||||||||||||||||||||
Xplor file |
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