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- PDB-1pbb: CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COM... -
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Basic information
Entry | Database: PDB / ID: 1pbb | ||||||
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Title | CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING | ||||||
![]() | P-HYDROXYBENZOATE HYDROXYLASE | ||||||
![]() | OXIDOREDUCTASE | ||||||
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 Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Schreuder, H.A. / Mattevi, A. / Hol, W.G.J. | ||||||
![]() | ![]() 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. #1: ![]() Title: Crystal Structure of the Reduced Form of P-Hydroxybenzoate Hydroxylase Refined at 2.3 Angstroms Resolution Authors: Schreuder, H.A. / Van Der Laan, J.M. / Swarte, M.B.A. / Kalk, K.H. / Hol, W.G.J. / Drenth, J. #2: ![]() Title: The Influence of Purification and Protein Heterogeneity on the Crystallization of P-Hydroxybenzoate Hydroxylase Authors: Van Der Laan, J.M. / Swarte, M.B.A. / Groendijk, H. / Hol, W.G.J. / Drenth, J. #3: ![]() Title: The Coenzyme Analogue Adenosine 5-Diphosphoribose Displaces Fad in the Active Site of P-Hydroxybenzoate Hydroxylase. An X-Ray Crystallographic Investigation Authors: Van Der Laan, J.M. / Schreuder, H.A. / Swarte, M.B.A. / Wierenga, R.K. / Kalk, K.H. / Hol, W.G.J. / Drenth, J. #4: ![]() Title: Analysis of the Active Site of the Flavoprotein P-Hydroxybenzoate Hydroxylase and Some Ideas with Respect to its Reaction Mechanism Authors: Schreuder, H.A. / Hol, W.G.J. / Drenth, J. #5: ![]() Title: Crystal Structure of the P-Hydroxybenzoate Hydroxylase-Substrate Complex Refined at 1.9 Angstroms Resolution. Analysis of the Enzyme-Substrate and Enzyme-Product Complexes Authors: Schreuder, H.A. / Prick, P.A.J. / Wierenga, R.K. / Vriend, G. / Wilson, K.S. / Hol, W.G.J. / Drenth, J. #6: ![]() Title: Molecular Modeling Reveals the Possible Importance of a Carbonyl Oxygen Binding Pocket for the Catalytic Mechanism of P-Hydroxybenzoate Hydroxylase Authors: Schreuder, H.A. / Hol, W.G.J. / Drenth, J. #7: ![]() Title: Crystal Structure of P-Hydroxybenzoate Hydroxylase Complexed with its Reaction Product 3,4-Dihydroxybenzoate Authors: Schreuder, H.A. / Van Der Laan, J.M. / Hol, W.G.J. / Drenth, J. #8: ![]() Title: Comparison of the Three-Dimensional Protein and Nucleotide Structure of the Fad-Binding Domain of P-Hydroxybenzoate Hydroxylase with the Fad-as Well as Nadph-Binding Domains of Glutathione Reductase Authors: Wierenga, R.K. / Drenth, J. / Schulz, G.E. #9: ![]() Title: Crystal Structure of P-Hydroxybenzoate Hydroxylase Authors: Wierenga, R.K. / De Jong, R.J. / Kalk, K.H. / Hol, W.G.J. / Drenth, J. #10: ![]() Title: Crystallization and Preliminary X-Ray Investigation of P-Hydroxybenzoate Hydroxylase from Pseudomonas Fluorescens Authors: Drenth, J. / Hol, W.G.J. / Wierenga, R.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 97.8 KB | Display | ![]() |
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PDB format | ![]() | 74 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 717.4 KB | Display | ![]() |
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Full document | ![]() | 723.2 KB | Display | |
Data in XML | ![]() | 18.7 KB | Display | |
Data in CIF | ![]() | 26.7 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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1 | ![]()
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 275 |
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Components
#1: Protein | Mass: 44364.508 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: P00438, 4-hydroxybenzoate 3-monooxygenase |
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#2: Chemical | ChemComp-FAD / |
#3: Chemical | ChemComp-DOB / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.58 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: free interface liquid-liquid diffusion | ||||||||||||||||||||||||||||||||||||
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: 2.5 Å / Num. obs: 15242 / % possible obs: 91.3 % / Rmerge(I) obs: 0.039 |
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Processing
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Refinement | Resolution: 2.5→8 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 14812 / Rfactor all: 0.158 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.53 |