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Open data
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Basic information
Entry | Database: PDB / ID: 1foh | ||||||
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Title | PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM | ||||||
![]() | PHENOL HYDROXYLASE | ||||||
![]() | FLAVIN / PHENOL HYDROXYLASE / MONOOXYGENASE / OXIDOREDUCTASE | ||||||
Function / homology | ![]() phenol-containing compound catabolic process / phenol 2-monooxygenase (NADPH) / phenol 2-monooxygenase activity / FAD binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Enroth, C. / Neujahr, H. / Schneider, G. / Lindqvist, Y. | ||||||
![]() | ![]() Title: The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis. Authors: Enroth, C. / Neujahr, H. / Schneider, G. / Lindqvist, Y. #1: ![]() Title: Crystallization and Preliminary X-Ray Analysis of Phenol Hydroxylase from Trichosporon Cutaneum Authors: Enroth, C. / Huang, W. / Waters, S. / Neujahr, H. / Lindqvist, Y. / Schneider, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 543.4 KB | Display | ![]() |
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PDB format | ![]() | 443.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 693.4 KB | Display | ![]() |
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Full document | ![]() | 775.2 KB | Display | |
Data in XML | ![]() | 61.7 KB | Display | |
Data in CIF | ![]() | 95.6 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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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 75197.641 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-FAD / #3: Chemical | ChemComp-IPH / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 47.3 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.5 / Details: pH 8.5 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 1, 1997 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9997 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→25 Å / Num. obs: 118897 / % possible obs: 98.1 % / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Biso Wilson estimate: 35.5 Å2 / Rsym value: 0.095 / Net I/σ(I): 7.8 |
Reflection shell | Resolution: 2.4→2.49 Å / Mean I/σ(I) obs: 2 / Rsym value: 0.335 / % possible all: 94.1 |
Reflection | *PLUS Rmerge(I) obs: 0.095 |
Reflection shell | *PLUS % possible obs: 94.1 % / Rmerge(I) obs: 0.335 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 41.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati d res low obs: 12 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→12 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.217 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |