+Open data
-Basic information
Entry | Database: PDB / ID: 1hj3 | ||||||
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Title | Cytochrome cd1 Nitrite Reductase, dioxygen complex | ||||||
Components | Nitrite reductase | ||||||
Keywords | OXIDOREDUCTASE / ENZYME / NITRITE REDUCTASE | ||||||
Function / homology | Function and homology information hydroxylamine reductase / hydroxylamine reductase activity / nitrite reductase (NO-forming) / nitrite reductase (NO-forming) activity / electron transfer activity / periplasmic space / heme binding / metal ion binding Similarity search - Function | ||||||
Biological species | Paracoccus pantotrophus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Sjogren, T. / Hajdu, J. | ||||||
Citation | Journal: J. Biol. Chem. / Year: 2001 Title: Structure of the bound dioxygen species in the cytochrome oxidase reaction of cytochrome cd1 nitrite reductase. Authors: Sjogren, T. / Hajdu, J. #1: Journal: Nature / Year: 1997 Title: Haem Ligand-Switching During Catalysis in Crystals of a Nitrogen Cycle Enzyme Authors: Williams, P.A. / Fulop, V. / Garman, E.F. / Saunders, N.F.W. / Ferguson, S.J. / Hajdu, J. #2: Journal: Cell(Cambridge,Mass.) / Year: 1995 Title: The Anatomy of a Bifunctional Enzyme: Structural Basis for Reduction of Oxygen to Water and Synthesis of Nitric Oxide by Cytochrome Cd1 Authors: Fulop, V. / Moir, J.W.B. / Saunders, N.F.W. / Ferguson, S.J. / Hajdu, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hj3.cif.gz | 244.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hj3.ent.gz | 193.8 KB | Display | PDB format |
PDBx/mmJSON format | 1hj3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hj/1hj3 ftp://data.pdbj.org/pub/pdb/validation_reports/hj/1hj3 | HTTPS FTP |
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-Related structure data
Related structure data | 1hj4C 1hj5C 1aofS 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
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 62546.539 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: ORGANISM FORMERLY KNOWN AS THIOSPHAERA PANTOTROPHA / Source: (natural) Paracoccus pantotrophus (bacteria) / Cellular location: PERIPLASM References: UniProt: P72181, nitrite reductase (NO-forming), hydroxylamine reductase |
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-Non-polymers , 6 types, 805 molecules
#2: Chemical | #3: Chemical | #4: Chemical | #5: Chemical | #6: Chemical | ChemComp-OXY / | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 11 |
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-Sample preparation
Crystal | Density Matthews: 2.52 Å3/Da / Density % sol: 51 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / pH: 7 Details: 2.3 M AMMONIUM SULFATE 50MM POTASSIUM PHOSPHATE PH 7.0 CRYSTALS WERE REDUCED USING 20MM SODIUM DITHIONITE. THE CRYSTAL WAS TRANSFERRED TO A SOLUTION CONTAINING 2.3 M AMMONIUM SULFATE, 50 MM ...Details: 2.3 M AMMONIUM SULFATE 50MM POTASSIUM PHOSPHATE PH 7.0 CRYSTALS WERE REDUCED USING 20MM SODIUM DITHIONITE. THE CRYSTAL WAS TRANSFERRED TO A SOLUTION CONTAINING 2.3 M AMMONIUM SULFATE, 50 MM PHOSPAHTE BUFFER PH 7 AND 15 % GLYCEROL. O2 WAS INTRODUCED UNDER 15 ATM PRESSURE FOR 2 MINUTES AT -20 DEGREES. THE DATA SET IS COMPOSED 10 DEGREE WEDGES OF DATA FROM 11 IDENTICAL CRYSTALS. | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 15 ℃ / Method: vapor diffusion, hanging drop / Details: Fulop, V., (1993) J. Mol. Biol., 232, 1211. | ||||||||||||||||||||||||||||||
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: ESRF / Beamline: ID14-2 / Wavelength: 0.933 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 29, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→30 Å / Num. obs: 135637 / % possible obs: 85.3 % / Observed criterion σ(I): 0 / Redundancy: 2.1 % / Biso Wilson estimate: 17.714 Å2 / Rmerge(I) obs: 0.046 / Rsym value: 0.046 / Net I/σ(I): 14.1 |
Reflection shell | Resolution: 1.6→1.66 Å / Rmerge(I) obs: 0.175 / Mean I/σ(I) obs: 2.9 / Rsym value: 0.175 / % possible all: 85.4 |
Reflection shell | *PLUS % possible obs: 85.4 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1AOF Resolution: 1.6→30 Å / SU B: 1.737 / SU ML: 0.061 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.098 / ESU R Free: 0.094 Details: IN MONOMER A RESIDUES A 1 - A 16 AND A 108- A 114 ARE DISORDERED IN THE STRUCTURE AND WERE NOT MODELLED. IN MONOMER B THE N-TERMINAL RESIDUES B 1 - B 26 ARE DISORDERED IN THE STRUCTURE AND ...Details: IN MONOMER A RESIDUES A 1 - A 16 AND A 108- A 114 ARE DISORDERED IN THE STRUCTURE AND WERE NOT MODELLED. IN MONOMER B THE N-TERMINAL RESIDUES B 1 - B 26 ARE DISORDERED IN THE STRUCTURE AND WERE NOT MODELLED. THE DIOXYGEN SPECIES FORMED BY INCUBATING THE REDUCED CRYSTAL WITH OXYGEN WAS REDUCED UPON EXPOSURE TO X-RAYS AS JUDGED BY MICROSPECTROSCOPY AND X-RAY CRYSTALLOGRAPHY. IN ORDER TO CAPTURE THIS STRUCTURE DATA FROM 11 DIFFERENT CRYSTALS WERE USED
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Refinement step | Cycle: LAST / Resolution: 1.6→30 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.196 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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