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- PDB-1iuw: P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1iuw | ||||||
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Title | P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH 7.4 | ||||||
![]() | P-HYDROXYBENZOATE HYDROXYLASE | ||||||
![]() | OXIDOREDUCTASE / AROMATIC HYDROCARBONS CATABOLISM / OXIDOREDUCATASE | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Gatti, D.L. / Entsch, B. / Ballou, D.P. / Ludwig, M.L. | ||||||
![]() | ![]() 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: ![]() 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: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 98.2 KB | Display | ![]() |
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PDB format | ![]() | 74.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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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 7.4 STRUCTURE / Source: (gene. exp.) ![]() ![]() ![]() ![]() 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: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 31.9 % Description: THE DATA SET USED IN THE REFINEMENT WAS OBTAINED BY MERGING TWO DATA SETS (PARAMETERS FOR EACH SET ARE SEPARATED BY A SEMICOLON. THE MERGING R VALUE BETWEEN THESE TWO DATA SETS IS 0.079. | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.4 / Details: pH 7.4 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4-23 ℃ / 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: 31420 / % possible obs: 99.14 % / Observed criterion σ(I): 1 / Redundancy: 11.6 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 7.95 |
Reflection shell | Resolution: 2→2.15 Å / Redundancy: 7.8 % / Rmerge(I) obs: 0.284 / Mean I/σ(I) obs: 3.1 / % possible all: 98.82 |
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Processing
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Refinement | Resolution: 2→15 Å / σ(F): 0 Details: MODIFIED CYSTEINE WITH ADDITIONAL ELECTRON DENSITY NEAR THE SULFUR AT X=4.90 Y=106.61 Z=72.18. THE TYPE OF CHEMICAL MODIFICATION CANNOT BE UNAMBIGUOUSLY DETERMINED FROM THE ELECTRON DENSITY. ...Details: MODIFIED CYSTEINE WITH ADDITIONAL ELECTRON DENSITY NEAR THE SULFUR AT X=4.90 Y=106.61 Z=72.18. THE TYPE OF CHEMICAL MODIFICATION CANNOT BE UNAMBIGUOUSLY DETERMINED FROM THE ELECTRON DENSITY. THE SIDE CHAINS OF RESIDUES 135, 136, 144, 146, 147, 173, 391, 392, 393, 394 ARE NOT ORDERED. 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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