+Open data
-Basic information
Entry | Database: PDB / ID: 5cp4 | ||||||
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Title | CRYOGENIC STRUCTURE OF P450CAM | ||||||
Components | CYTOCHROME P450CAM | ||||||
Keywords | OXIDOREDUCTASE / P450 / MONOOXYGENASE / HEME ENZYME / ELECTRON TRANSPORT | ||||||
Function / homology | Function and homology information camphor 5-monooxygenase / camphor 5-monooxygenase activity / (+)-camphor catabolic process / iron ion binding / heme binding / cytoplasm Similarity search - Function | ||||||
Biological species | Pseudomonas putida (bacteria) | ||||||
Method | X-RAY DIFFRACTION / molecular replacement / Resolution: 1.75 Å | ||||||
Authors | Li, H. / Poulos, T.L. | ||||||
Citation | Journal: Biochemistry / Year: 1998 Title: Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect. Authors: Vidakovic, M. / Sligar, S.G. / Li, H. / Poulos, T.L. #1: Journal: J.Mol.Biol. / Year: 1987 Title: High-Resolution Crystal Structure of Cytochrome P450Cam Authors: Poulos, T.L. / Finzel, B.C. / Howard, A.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5cp4.cif.gz | 128.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5cp4.ent.gz | 103.4 KB | Display | PDB format |
PDBx/mmJSON format | 5cp4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cp/5cp4 ftp://data.pdbj.org/pub/pdb/validation_reports/cp/5cp4 | HTTPS FTP |
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-Related structure data
Related structure data | 6cp4C 2cppS 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, 1 molecules A
#1: Protein | Mass: 46588.879 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas putida (bacteria) / Production host: Escherichia coli (E. coli) / Strain (production host): DH5A / References: UniProt: P00183, camphor 5-monooxygenase |
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-Non-polymers , 5 types, 413 molecules
#2: Chemical | ChemComp-K / | ||
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#3: Chemical | ChemComp-HEM / | ||
#4: Chemical | ChemComp-CAM / | ||
#5: Chemical | #6: 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: 2.15 Å3/Da / Density % sol: 48 % |
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Crystal grow | pH: 7 / Details: pH 7.0 |
Crystal grow | *PLUS Method: other / Details: Poulos, T.L., (1996) Methods Enzymol., 272, 358. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418 |
Detector | Type: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR / Date: Apr 1, 1996 / Details: MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→30 Å / Num. obs: 31326 / % possible obs: 89.7 % / Observed criterion σ(I): 0 / Redundancy: 4 % / Rsym value: 0.058 |
Reflection shell | Resolution: 1.75→1.9 Å / % possible all: 54.7 |
Reflection | *PLUS Num. obs: 37112 / Num. measured all: 179587 / Rmerge(I) obs: 0.058 |
Reflection shell | *PLUS % possible obs: 54.7 % |
-Processing
Software |
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Refinement | Method to determine structure: molecular replacement Starting model: PDB ENTRY 2CPP Resolution: 1.75→10 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 1.75→10 Å
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Refine LS restraints |
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