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- PDB-2pnj: Crystal structure of human ferrochelatase mutant with Phe 337 rep... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2pnj | ||||||
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Title | Crystal structure of human ferrochelatase mutant with Phe 337 replaced by Ala | ||||||
![]() | Ferrochelatase, mitochondrial | ||||||
![]() | LYASE / FERROCHELATASE / F337A Mutant / FE2S2 CLUSTER / HEME BIOSYNTHESIS / PROTOHEME FERRO-LYASE / MATURE LENGTH / PROTEOLYTICALLY PROCESSED MITOCHONDRIAL INNER MEMBRANE PROTEIN | ||||||
Function / homology | ![]() 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 / Mitochondrial protein degradation / cholesterol metabolic process / cellular response to dexamethasone stimulus / erythrocyte differentiation / 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 | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Dailey, H.A. / Wu, C.-K. / Horanyi, P. / Medlock, A.E. / Najahi-Missaoui, W. / Burden, A.E. / 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 | ![]() | 163.5 KB | Display | ![]() |
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PDB format | ![]() | 129 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2po5C ![]() 2po7C ![]() 1hrkS 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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: ARG / Beg label comp-ID: ARG / End auth comp-ID: LEU / End label comp-ID: LEU / Refine code: 4 / Auth seq-ID: 65 - 423 / Label seq-ID: 1 - 359
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Components
#1: Protein | Mass: 41058.254 Da / Num. of mol.: 2 / Fragment: Mature Protein / Mutation: R115L, F337A 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: 2.81 Å3/Da / Density % sol: 56.23 % |
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Crystal grow | Temperature: 291 K / Method: microbatch / pH: 6.5 Details: MICROBATCH UNDER OIL (70:30 PARAFFIN/SILICONE OIL MIXTURE) METHO USING 2 microliter DROPS CONTAINING EQUAL VOLUMES OF PROTEIN SOLUTION (64 MG/ML IN 50 MM TRIS MOPS, 0.1M KCL, 1% NA-CHOLATE, ...Details: MICROBATCH UNDER OIL (70:30 PARAFFIN/SILICONE OIL MIXTURE) METHO USING 2 microliter DROPS CONTAINING EQUAL VOLUMES OF PROTEIN SOLUTION (64 MG/ML IN 50 MM TRIS MOPS, 0.1M KCL, 1% NA-CHOLATE, 250 MM IMIDAZOLE, PH 8.1) AND PRECIPITANT SOLUTION (0.2 M SODIUM ACETAT TRI HYDRATE, 0.1 M SODIUM CACODYLATE, PH 6.5 IN 30%W/V POLYETHYL GLYCOL 8000 (HAMPTON CRYSTAL SCREEN I-28, HAMPTON RESEARCH), pH 6.50, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Nov 18, 2005 / Details: ROSENBAUM | |||||||||
Radiation | Monochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 2→50 Å / Num. obs: 58933 / % possible obs: 90.1 % / Redundancy: 17.5 % / Rmerge(I) obs: 0.057 / Net I/σ(I): 25.23 | |||||||||
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 10 % / Rmerge(I) obs: 0.242 / Mean I/σ(I) obs: 3.39 / % possible all: 98.2 |
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Processing
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: 1HRK Resolution: 2.35→43.44 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.91 / SU B: 6.661 / SU ML: 0.165 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.332 / ESU R Free: 0.251 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 25.034 Å2
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Refinement step | Cycle: LAST / Resolution: 2.35→43.44 Å
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Refine LS restraints |
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Refine LS restraints NCS | Dom-ID: 1 / Auth asym-ID: A / Ens-ID: 1 / Number: 2811 / Refine-ID: X-RAY DIFFRACTION
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LS refinement shell | Resolution: 2.35→2.411 Å / Total num. of bins used: 20
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