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Yorodumi- PDB-1iux: P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1iux | ||||||
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Title | P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH 9.4 | ||||||
Components | P-HYDROXYBENZOATE HYDROXYLASE | ||||||
Keywords | OXIDOREDUCTASE / AROMATIC HYDROCARBONS CATABOLISM / OXIDOREDUCATASE | ||||||
Function / homology | Function and homology information 4-hydroxybenzoate 3-monooxygenase (NADPH) activity / 4-hydroxybenzoate 3-monooxygenase / 4-hydroxybenzoate 3-monooxygenase activity / benzoate catabolic process via hydroxylation / FAD binding / flavin adenine dinucleotide binding / oxidoreductase activity Similarity search - Function | ||||||
Biological species | Pseudomonas aeruginosa (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Gatti, D.L. / Entsch, B. / Ballou, D.P. / Ludwig, M.L. | ||||||
Citation | Journal: Biochemistry / Year: 1996 Title: pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis. Authors: Gatti, D.L. / Entsch, B. / Ballou, D.P. / Ludwig, M.L. #1: Journal: Biochemistry / Year: 1994 Title: Crystal Structures of Wild-Type P-Hydroxybenzoate Hydroxylase Complexed with 4-Aminobenzoate,2,4-Dihydroxybenzoate, and 2-Hydroxy-4-Aminobenzoate and of the Tyr222Ala Mutant Complexed with 2- ...Title: Crystal Structures of Wild-Type P-Hydroxybenzoate Hydroxylase Complexed with 4-Aminobenzoate,2,4-Dihydroxybenzoate, and 2-Hydroxy-4-Aminobenzoate and of the Tyr222Ala Mutant Complexed with 2-Hydroxy-4-Aminobenzoate. Evidence for a Proton Channel and a New Binding Mode of the Flavin Ring Authors: Schreuder, H.A. / Mattevi, A. / Obmolova, G. / Kalk, K.H. / Hol, W.G. / Van Der Bolt, F.J. / Van Berkel, W.J. #2: Journal: Biochemistry / Year: 1994 Title: Crystal Structures of Mutant Pseudomonas Aeruginosa P-Hydroxybenzoate Hydroxylases:The Tyr201Phe, Tyr385Phe and Asn300Asp Variants Authors: Lah, M.S. / Palfey, B.A. / Schreuder, H.A. / Ludwig, M.L. #3: Journal: J.Biol.Chem. / Year: 1991 Title: Catalytic Function of Tyrosine Residues in Para-Hydroxybenzoate Hydroxylase as Determined by the Study of Site-Directed Mutants Authors: Entsch, B. / Palfey, B.A. / Ballou, D.P. / Massey, V. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1iux.cif.gz | 98 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1iux.ent.gz | 74.2 KB | Display | PDB format |
PDBx/mmJSON format | 1iux.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1iux_validation.pdf.gz | 477.4 KB | Display | wwPDB validaton report |
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Full document | 1iux_full_validation.pdf.gz | 482.5 KB | Display | |
Data in XML | 1iux_validation.xml.gz | 9.7 KB | Display | |
Data in CIF | 1iux_validation.cif.gz | 15.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/iu/1iux ftp://data.pdbj.org/pub/pdb/validation_reports/iu/1iux | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 44382.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: PH 9.4 STRUCTURE / Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Strain: PAO1 / Gene: POBA / Plasmid: PIE130 / Gene (production host): POBA / Production host: Escherichia coli (E. coli) / Strain (production host): JM105 References: UniProt: P20586, 4-hydroxybenzoate 3-monooxygenase |
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#2: Chemical | ChemComp-FAD / |
#3: Chemical | ChemComp-PHB / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 31.9 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 9.4 / Details: pH 9.4 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4-23 ℃ / pH: 7.4 / Method: interface diffusion | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Details: 0.5 MM COLLIMATOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→15 Å / Num. obs: 31069 / % possible obs: 98.3 % / Observed criterion σ(I): 1 / Redundancy: 7.58 % / Rmerge(I) obs: 0.295 / Net I/σ(I): 7.8 |
Reflection shell | Resolution: 2→2.15 Å / Redundancy: 4.55 % / Rmerge(I) obs: 0.295 / Mean I/σ(I) obs: 0.0105 / % possible all: 94.08 |
-Processing
Software |
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Refinement | Resolution: 2→15 Å / σ(F): 0 Details: THE SEGMENT PRO 293 - ALA 296 IS PRESENT IN TWO CONFORMATIONS. CYS 116: MODIFIED CYSTEINE WITH ADDITIONAL ELECTRON DENSITY NEAR THE SULFUR AT X=5.47 Y=107.86 Z=71.44. THE TYPE OF CHEMICAL ...Details: THE SEGMENT PRO 293 - ALA 296 IS PRESENT IN TWO CONFORMATIONS. CYS 116: MODIFIED CYSTEINE WITH ADDITIONAL ELECTRON DENSITY NEAR THE SULFUR AT X=5.47 Y=107.86 Z=71.44. THE TYPE OF CHEMICAL MODIFICATION CANNOT BE UNAMBIGUOUSLY DETERMINED FROM THE ELECTRON DENSITY. SIDE CHAIN OF RESIDUES 136, 173, 393, 394 NOT ORDERED. THE THE MODEL IS DERIVED FROM A COMBINATION OF FIT TO RESIDUAL DENSITY AND ENERGY MINIMIZATION.
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Refinement step | Cycle: LAST / Resolution: 2→15 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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