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Open data
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Basic information
Entry | Database: PDB / ID: 6cp4 | ||||||
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Title | P450CAM D251N MUTANT | ||||||
![]() | CYTOCHROME P450CAM | ||||||
![]() | OXIDOREDUCTASE / P450 / MONOOXYGENASE / HEME ENZYME / ELECTRON TRANSPORT | ||||||
Function / homology | ![]() 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 | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Li, H. / Poulos, T.L. | ||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 130.4 KB | Display | ![]() |
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PDB format | ![]() | 101 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 493.8 KB | Display | ![]() |
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Full document | ![]() | 497.1 KB | Display | |
Data in XML | ![]() | 10 KB | Display | |
Data in CIF | ![]() | 17 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5cp4C ![]() 2cppS 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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1 |
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Unit cell |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 46587.895 Da / Num. of mol.: 1 / Mutation: D251N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Non-polymers , 5 types, 374 molecules ![](data/chem/img/K.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/CAM.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/CAM.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-K / |
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#3: Chemical | ChemComp-HEM / |
#4: Chemical | ChemComp-CAM / |
#5: Chemical | ChemComp-GOL / |
#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 1, 1997 / Details: MIRRORS |
Radiation | Monochromator: YES / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→30 Å / Num. obs: 31326 / % possible obs: 96 % / Observed criterion σ(I): 0 / Redundancy: 3 % / Rsym value: 0.049 |
Reflection shell | Resolution: 1.9→1.93 Å / Redundancy: 2 % / % possible all: 96.6 |
Reflection | *PLUS Num. measured all: 98277 / Rmerge(I) obs: 0.049 |
Reflection shell | *PLUS % possible obs: 96.6 % / Mean I/σ(I) obs: 5.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2CPP Resolution: 1.9→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: 1.9→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.2 / Rfactor Rwork: 0.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |