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- PDB-4cpp: CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4cpp | ||||||
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Title | CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATION | ||||||
![]() | CYTOCHROME P450-CAM | ||||||
![]() | OXIDOREDUCTASE(OXYGENASE) | ||||||
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 | ![]() | ||||||
![]() | Raag, R. / Poulos, T.L. | ||||||
![]() | ![]() Title: Crystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation. Authors: Raag, R. / Poulos, T.L. #1: ![]() Title: X-Ray Crystallographic Structural Studies of Cytochrome P450-Cam+ Authors: Raag, R. / Poulos, T.L. #2: ![]() Title: Crystal Structure of the Carbon Monoxy-Substrate-Cytochrome P450-Cam Ternary Complex Authors: Raag, R. / Poulos, T.L. #3: ![]() Title: The Structural Basis for Substrate-Induced Changes in Redox Potential and Spin Equilibrium in Cytochrome P450(Cam) Authors: Raag, R. / Poulos, T.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 98 KB | Display | ![]() |
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PDB format | ![]() | 75.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 490.2 KB | Display | ![]() |
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Full document | ![]() | 504.3 KB | Display | |
Data in XML | ![]() | 11.7 KB | Display | |
Data in CIF | ![]() | 18.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Atom site foot note | 1: RESIDUES PRO 89, PRO 100, PRO 106 ARE CIS PROLINES. |
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Components
#1: Protein | Mass: 46588.879 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Chemical | ChemComp-HEM / |
#3: Chemical | ChemComp-ADM / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44.16 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7 / Method: other | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Num. measured all: 144737 / Rmerge(I) obs: 0.079 |
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Processing
Software | Name: PROFFT / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.184 / Highest resolution: 2.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.11 Å
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Refine LS restraints |
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Refinement | *PLUS Num. reflection all: 20548 / Num. reflection obs: 15174 / σ(I): 2 / Rfactor obs: 0.184 / Highest resolution: 2.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: p_dihedral_angle_d / Dev ideal: 0.037 |