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- PDB-1cp4: FORMATION, CRYSTAL STRUCTURE, AND REARRANGEMENT OF A CYTOCHROME P... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cp4 | ||||||
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Title | FORMATION, CRYSTAL STRUCTURE, AND REARRANGEMENT OF A CYTOCHROME P450-CAM IRON-PHENYL COMPLEX | ||||||
![]() | 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: Formation, crystal structure, and rearrangement of a cytochrome P-450cam iron-phenyl complex. Authors: Raag, R. / Swanson, B.A. / Poulos, T.L. / Ortiz de Montellano, P.R. #1: ![]() Title: X-Ray Crystallographic Structural Studies of Cytochrome P450-Cam+ Authors: Raag, R. / Poulos, T.L. #2: ![]() Title: Crystal Structures of Cytochrome P450-Cam Complexed with Camphane, Thiocamphor, and Adamantane: Factors Controlling P450 Substrate Hydroxylation Authors: Raag, R. / Poulos, T.L. #3: ![]() Title: Crystal Structure of the Carbon Monoxy-Substrate-Cytochrome P450-Cam Ternary Complex Authors: Raag, R. / Poulos, T.L. #4: ![]() 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 | ![]() | 97.7 KB | Display | ![]() |
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PDB format | ![]() | 75.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 482.4 KB | Display | ![]() |
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Full document | ![]() | 495.8 KB | Display | |
Data in XML | ![]() | 11.7 KB | Display | |
Data in CIF | ![]() | 18.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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, AND 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-BNZ / |
#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 Temperature: 12-15 ℃ / Method: batch method / Details: took Poulos et al., 1982 from original paper | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.87 Å / % possible obs: 55 % / Num. measured all: 128716 / Rmerge(I) obs: 0.074 |
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Processing
Software | Name: PROFFT / Classification: refinement | ||||||||||||
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Refinement | Rfactor obs: 0.199 / Highest resolution: 1.9 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.9 Å
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Refine LS restraints |
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Software | *PLUS Name: PROFFT / Classification: refinement | ||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å / Num. reflection all: 27666 / Num. reflection obs: 20765 / Rfactor obs: 0.199 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS Type: p_dihedral_angle_d / Dev ideal: 0.036 |