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- PDB-1cpt: CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 A... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cpt | ||||||
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Title | CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTION | ||||||
![]() | CYTOCHROME P450-TERP | ||||||
![]() | OXIDOREDUCTASE(OXYGENASE) | ||||||
Function / homology | ![]() Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen / 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 | ![]() | ||||||
![]() | Hasemann, C.A. / Ravichandran, K.G. / Peterson, J.A. / Deisenhofer, J. | ||||||
![]() | ![]() Title: Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution. Authors: Hasemann, C.A. / Ravichandran, K.G. / Peterson, J.A. / Deisenhofer, J. #1: ![]() Title: Crystallization and Preliminary X-Ray Diffraction Analysis of P450-Terp and the Hemoprotein Domain of P450-Bm-3, Enzymes Belonging to Two Distinct Classes of the Cytochrome P450 Superfamily Authors: Boddupalli, S.S. / Hasemann, C.A. / Ravichandran, K.G. / Lu, J.-Y. / Goldsmith, E.J. / Deisenhofer, J. / Peterson, J.A. #2: ![]() Title: Cytochrome P450-Terp: Isolation and Purification of the Protein and Cloning and Sequencing of its Operon Authors: Peterson, J.A. / Lu, J.-Y. / Geisselsoder, J. / Graham-Lorence, S. / Carmona, C. / Witney, F. / Lorence, M.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 100.3 KB | Display | ![]() |
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PDB format | ![]() | 76.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 806.8 KB | Display | ![]() |
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Full document | ![]() | 818.1 KB | Display | |
Data in XML | ![]() | 20.1 KB | Display | |
Data in CIF | ![]() | 29.1 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: CIS PROLINE - PRO 108 2: FOR RESIDUE 207 NO DENSITY WAS SEEN FOR SIDE CHAIN ATOMS BEYOND CA. 3: ASPARTATES 236 AND 253 WERE MODELLED IN ALTERNATE CONFORMATIONS. 4: CIS PROLINE - PRO 364 / 5: WATER 440 IS AN AXIAL LIGAND TO THE HEME IRON. |
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Components
#1: Protein | Mass: 47977.207 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: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.31 Å3/Da / Density % sol: 62.83 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.8 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 2.2 Å / Num. obs: 24645 / % possible obs: 69 % / Num. measured all: 78920 / Rmerge(I) obs: 0.056 |
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Processing
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Refinement | Rfactor Rwork: 0.189 / Rfactor obs: 0.189 / Highest resolution: 2.3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.3 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 6 Å / Num. reflection all: 21470 / Num. reflection obs: 21263 / σ(F): 1 / Rfactor all: 0.205 / Rfactor obs: 0.189 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 40.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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