+Open data
-Basic information
Entry | Database: PDB / ID: 1noo | ||||||
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Title | CYTOCHROME P450-CAM COMPLEXED WITH 5-EXO-HYDROXYCAMPHOR | ||||||
Components | CYTOCHROME P450-CAM | ||||||
Keywords | OXIDOREDUCTASE (OXYGENASE) / MONOOXYGENASE | ||||||
Function / homology | Function and homology information camphor 5-monooxygenase / camphor 5-monooxygenase activity / (+)-camphor catabolic process / cholest-4-en-3-one 26-monooxygenase activity / steroid hydroxylase activity / cholesterol catabolic process / iron ion binding / heme binding / cytoplasm Similarity search - Function | ||||||
Biological species | Pseudomonas putida (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.2 Å | ||||||
Authors | Li, H.Y. / Poulos, T.L. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 1995 Title: Crystal Structure of Cytochrome P450-Cam Complexed with its Catalytic Product, 5-Exo-Hydroxycamphor Authors: Li, H. / Narasimhulu, S. / Havran, L.M. / Winkler, J.D. / Poulos, T.L. #1: Journal: J.Mol.Biol. / Year: 1987 Title: High-Resolution Crystal Structure of Cytochrome P450-Cam 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 | 1noo.cif.gz | 97.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1noo.ent.gz | 74.1 KB | Display | PDB format |
PDBx/mmJSON format | 1noo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1noo_validation.pdf.gz | 809.6 KB | Display | wwPDB validaton report |
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Full document | 1noo_full_validation.pdf.gz | 813.2 KB | Display | |
Data in XML | 1noo_validation.xml.gz | 18.9 KB | Display | |
Data in CIF | 1noo_validation.cif.gz | 27.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/no/1noo ftp://data.pdbj.org/pub/pdb/validation_reports/no/1noo | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 89 / 2: CIS PROLINE - PRO 100 / 3: CIS PROLINE - PRO 106 |
-Components
#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) / References: UniProt: P00183, camphor 5-monooxygenase |
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#2: Chemical | ChemComp-HEM / |
#3: Chemical | ChemComp-CAH / |
#4: 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: 2.22 Å3/Da / Density % sol: 44.57 % |
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Crystal grow | *PLUS Temperature: 7 ℃ / Method: free interface diffusion method |
Components of the solutions | *PLUS Conc.: 50 mM / Common name: dithiothreitol |
-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Wavelength: 1.5418 Å |
Detector | Type: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR / Date: Oct 25, 1994 |
Radiation | 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: 20570 / % possible obs: 94 % / Redundancy: 4 % / Rmerge(I) obs: 0.0975 |
Reflection | *PLUS Rmerge(I) obs: 0.0975 |
-Processing
Software |
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Refinement | Resolution: 2.2→10 Å / σ(F): 2
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Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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