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- PDB-1coy: CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE COMPLEXED WITH A STEROID... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1coy | ||||||
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Title | CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE COMPLEXED WITH A STEROID SUBSTRATE. IMPLICATIONS FOR FAD DEPENDENT ALCOHOL OXIDASES | ||||||
![]() | CHOLESTEROL OXIDASE | ||||||
![]() | OXIDOREDUCTASE(OXYGEN RECEPTOR) | ||||||
Function / homology | ![]() cholesterol oxidase / cholesterol oxidase activity / steroid Delta-isomerase / steroid delta-isomerase activity / cholesterol catabolic process / flavin adenine dinucleotide binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Li, J. / Vrielink, A. / Brick, P. / Blow, D.M. | ||||||
![]() | ![]() Title: Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases. Authors: Li, J. / Vrielink, A. / Brick, P. / Blow, D.M. #1: ![]() Title: Crystal Structure of Cholesterol Oxidase from Brevibacterium Sterolicum Refined at 1.8 Angstroms Resolution Authors: Vrielink, A. / Lloyd, L.F. / Blow, D.M. #2: ![]() Title: Sequence of Gene Chob Encoding Cholesterol Oxidase of Brevibacterium Sterolicum: Comparison with Choa of Streptomyces Sp. Sa-Coo Authors: Ohta, T. / Fujishiro, K. / Yamaguchi, K. / Tamura, Y. / Aisaka, K. / Uwajima, T. / Hasegawa, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 118.1 KB | Display | ![]() |
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PDB format | ![]() | 89.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 969.3 KB | Display | ![]() |
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Full document | ![]() | 971.6 KB | Display | |
Data in XML | ![]() | 23.9 KB | Display | |
Data in CIF | ![]() | 36.1 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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Components
#1: Protein | Mass: 54891.742 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Chemical | ChemComp-AND / |
#3: Chemical | ChemComp-FAD / |
#4: Water | ChemComp-HOH / |
Nonpolymer details | THE STRUCTURE CONTAINS AN FAD COFACTOR IN THE REDUCED FORM. THE FLAVIN RING SYSTEM OF THE FAD ...THE STRUCTURE CONTAINS AN FAD COFACTOR IN THE REDUCED FORM. THE FLAVIN RING SYSTEM OF THE FAD MOLECULE ADOPTS A SLIGHTLY TWISTED CONFORMATI |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.3 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 18 ℃ / 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: 1.8 Å / Num. obs: 46169 / % possible obs: 96.3 % / Num. measured all: 192439 / Rmerge(I) obs: 0.066 |
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Processing
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Refinement | Resolution: 1.8→10 Å / Rfactor Rwork: 0.159 / Rfactor obs: 0.159 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 44943 / Rfactor obs: 0.159 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 16.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.35 |