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Yorodumi- PDB-1n0i: Crystal Structure of Ferrochelatase with Cadmium bound at active site -
+Open data
-Basic information
Entry | Database: PDB / ID: 1n0i | ||||||
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Title | Crystal Structure of Ferrochelatase with Cadmium bound at active site | ||||||
Components | Ferrochelatase | ||||||
Keywords | LYASE / PI-HELIX | ||||||
Function / homology | Function and homology information coproporphyrin ferrochelatase / ferrochelatase activity / heme biosynthetic process / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Lecerof, D. / Fodje, M.N. / Leon, R.A. / Olsson, U. / Hansson, A. / Sigfridsson, E. / Ryde, U. / Hansson, M. / Al-Karadaghi, S. | ||||||
Citation | Journal: J.Biol.Inorg.Chem. / Year: 2003 Title: Metal binding to Bacillus subtilis ferrochelatase and interaction between metal sites Authors: Lecerof, D. / Fodje, M.N. / Leon, R.A. / Olsson, U. / Hansson, A. / Sigfridsson, E. / Ryde, U. / Hansson, M. / Al-Karadaghi, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1n0i.cif.gz | 84.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1n0i.ent.gz | 62 KB | Display | PDB format |
PDBx/mmJSON format | 1n0i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n0/1n0i ftp://data.pdbj.org/pub/pdb/validation_reports/n0/1n0i | HTTPS FTP |
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-Related structure data
Related structure data | 1ld3C 1dozS 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: 35389.707 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P32396, protoporphyrin ferrochelatase | ||||||
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#2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.26 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion / pH: 7.4 Details: PEG2000, magnesium chloride, tris, pH 7.4, VAPOR DIFFUSION, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8.5 / Method: vapor diffusion, hanging dropDetails: Hansson, M., (1995) Proteins: Struct.,Funct., Genet., 23, 607. | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: MAX II / Beamline: I711 / Wavelength: 1.02916 Å |
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Sep 19, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.02916 Å / Relative weight: 1 |
Reflection | Resolution: 2→26.1 Å / Num. all: 19585 / Num. obs: 19585 / % possible obs: 97.3 % / Observed criterion σ(I): 2 / Biso Wilson estimate: 7.9 Å2 |
Reflection shell | Resolution: 2→2.2 Å / Rmerge(I) obs: 0.258 / Num. unique all: 22104 / % possible all: 96.7 |
Reflection | *PLUS Lowest resolution: 26 Å / Rmerge(I) obs: 0.241 |
Reflection shell | *PLUS Lowest resolution: 2.13 Å / % possible obs: 97.1 % / Rmerge(I) obs: 0.289 / Mean I/σ(I) obs: 80 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1DOZ Resolution: 2→26.11 Å / Rfactor Rfree error: 0.006 / 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: 51.7138 Å2 / ksol: 0.381242 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→26.11 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.15 Å / Rfactor Rfree error: 0.019 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 26 Å / % reflection Rfree: 10 % | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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