+Open data
-Basic information
Entry | Database: PDB / ID: 1foh | ||||||
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Title | PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM | ||||||
Components | PHENOL HYDROXYLASE | ||||||
Keywords | FLAVIN / PHENOL HYDROXYLASE / MONOOXYGENASE / OXIDOREDUCTASE | ||||||
Function / homology | Function and homology information phenol-containing compound catabolic process / phenol 2-monooxygenase (NADPH) / phenol 2-monooxygenase activity / FAD binding Similarity search - Function | ||||||
Biological species | Trichosporon cutaneum (fungus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 2.4 Å | ||||||
Authors | Enroth, C. / Neujahr, H. / Schneider, G. / Lindqvist, Y. | ||||||
Citation | Journal: Structure / Year: 1998 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: Journal: J.Mol.Biol. / Year: 1994 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1foh.cif.gz | 543.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1foh.ent.gz | 443.9 KB | Display | PDB format |
PDBx/mmJSON format | 1foh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1foh_validation.pdf.gz | 693.4 KB | Display | wwPDB validaton report |
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Full document | 1foh_full_validation.pdf.gz | 775.2 KB | Display | |
Data in XML | 1foh_validation.xml.gz | 61.7 KB | Display | |
Data in CIF | 1foh_validation.cif.gz | 95.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fo/1foh ftp://data.pdbj.org/pub/pdb/validation_reports/fo/1foh | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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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.) Trichosporon cutaneum (fungus) / Cell line: 293 / Gene: PHYA / Plasmid: PRJ6C / Production host: Escherichia coli (E. coli) / Strain (production host): XL1-BLUE / References: UniProt: P15245, phenol 2-monooxygenase (NADPH) #2: Chemical | ChemComp-FAD / #3: Chemical | ChemComp-IPH / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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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: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.9997 |
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 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.4→12 Å / Cross valid method: R FREE / σ(F): 0
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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 |