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Yorodumi- PDB-1pxb: CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1pxb | ||||||
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Title | CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS | ||||||
Components | P-HYDROXYBENZOATE HYDROXYLASE | ||||||
Keywords | OXIDOREDUCTASE | ||||||
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: 2.3 Å | ||||||
Authors | Lah, M.S. / Palfey, B.A. / Schreuder, H.A. / Ludwig, M.L. | ||||||
Citation | 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. #1: Journal: Biochemistry / Year: 1994 Title: Changes in the Catalytic Properties of P-Hydroxybenzoate Hydroxylase Caused by the Mutation Asn300Asp Authors: Palfey, B.A. / Entsch, B. / 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 | 1pxb.cif.gz | 96.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1pxb.ent.gz | 72.6 KB | Display | PDB format |
PDBx/mmJSON format | 1pxb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1pxb_validation.pdf.gz | 477.8 KB | Display | wwPDB validaton report |
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Full document | 1pxb_full_validation.pdf.gz | 487.9 KB | Display | |
Data in XML | 1pxb_validation.xml.gz | 10.7 KB | Display | |
Data in CIF | 1pxb_validation.cif.gz | 16.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/px/1pxb ftp://data.pdbj.org/pub/pdb/validation_reports/px/1pxb | HTTPS FTP |
-Related structure data
-Links
-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 |
-Components
#1: Protein | Mass: 44366.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) 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: 2.6 Å3/Da / Density % sol: 52.64 % | |||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7.5 / Method: other | |||||||||||||||
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: 2.3 Å / Lowest resolution: 40 Å / Num. obs: 20499 / % possible obs: 98 % / Observed criterion σ(I): 6.63 / Redundancy: 4 % / Rmerge(I) obs: 0.123 |
-Processing
Software |
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Refinement | Resolution: 2.3→40 Å / σ(F): 0 Details: THE HYDROGEN BOND DISTANCE CUTOFF USED FOR THE TURNS IS 3.5 ANGSTROMS. THE CA(X) TO CA(X+4) DISTANCE IS LESS THAN 6.0 ANGSTROMS. THE ANGLES ARE FROM ROBSON AND GARNIER (1986) 'INTRODUCTION ...Details: THE HYDROGEN BOND DISTANCE CUTOFF USED FOR THE TURNS IS 3.5 ANGSTROMS. THE CA(X) TO CA(X+4) DISTANCE IS LESS THAN 6.0 ANGSTROMS. THE ANGLES ARE FROM ROBSON AND GARNIER (1986) 'INTRODUCTION TO PROTEINS AND PROTEIN ENGINEERING', ELSEVIER, AMSTERDAM. TYPE PHI2 PSI2 PHI3 PSI3 I -75(+-65) -30(+-40) -90(+-40) -15 TO 40 II -60(+-40) 120(+-40) 90(+-40) 0(+-40) III -75(+-65) -30(+-40) -60(+-40) -15 TO -70 I(PRIME) 75(+-65) 30(+-40) 90(+-40) -40 TO 15 II(PRIME) 60(+-40) -120(+-40) -90(+-40) 0(+-40) III(PRIME) 75(+-65) 30(+-40) 60(+-40) 15 TO 70
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Refinement step | Cycle: LAST / Resolution: 2.3→40 Å
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Refine LS restraints |
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