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Yorodumi- PDB-2y4r: CRYSTAL STRUCTURE OF 4-AMINO-4-DEOXYCHORISMATE LYASE FROM PSEUDOM... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2y4r | |||||||||
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Title | CRYSTAL STRUCTURE OF 4-AMINO-4-DEOXYCHORISMATE LYASE FROM PSEUDOMONAS AERUGINOSA | |||||||||
Components | 4-AMINO-4-DEOXYCHORISMATE LYASE | |||||||||
Keywords | LYASE / PARA-AMINOBENZOIC ACID / FOLATE BIOSYNTHESIS | |||||||||
Function / homology | Function and homology information 4-amino-4-deoxychorismate lyase activity / folic acid biosynthetic process / pyridoxal phosphate binding / cytosol Similarity search - Function | |||||||||
Biological species | PSEUDOMONAS AERUGINOSA (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 Å | |||||||||
Authors | O'Rourke, P.E.F. / Eadsforth, T.C. / Fyfe, P.K. / Shepard, S.M. / Agacan, M. / Hunter, W.N. | |||||||||
Citation | Journal: Plos One / Year: 2011 Title: Pseudomonas Aeruginosa 4-Amino-4-Deoxychorismate Lyase: Spatial Conservation of an Active Site Tyrosine and Classification of Two Types of Enzyme. Authors: O'Rourke, P.E.F. / Eadsforth, T.C. / Fyfe, P.K. / Shepherd, S.M. / Hunter, W.N. | |||||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2y4r.cif.gz | 139.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2y4r.ent.gz | 107.3 KB | Display | PDB format |
PDBx/mmJSON format | 2y4r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2y4r_validation.pdf.gz | 506.6 KB | Display | wwPDB validaton report |
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Full document | 2y4r_full_validation.pdf.gz | 522.1 KB | Display | |
Data in XML | 2y4r_validation.xml.gz | 30.1 KB | Display | |
Data in CIF | 2y4r_validation.cif.gz | 43.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y4/2y4r ftp://data.pdbj.org/pub/pdb/validation_reports/y4/2y4r | HTTPS FTP |
-Related structure data
Related structure data | 1et0S S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 32337.939 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: LYSINE 140 IS COVALENTLY LINKED TO A PYRIDOXAL PHOSPHATE COFACTOR Source: (gene. exp.) PSEUDOMONAS AERUGINOSA (bacteria) / Strain: PAO1 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)GOLD / References: UniProt: Q9HZN6, aminodeoxychorismate lyase |
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-Non-polymers , 8 types, 493 molecules
#2: Chemical | #3: Chemical | ChemComp-PG4 / #4: Chemical | #5: Chemical | #6: Chemical | #7: Chemical | #8: Chemical | #9: Water | ChemComp-HOH / | |
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-Details
Nonpolymer details | PYRIDOXAL-5'-PHOSPHATE (PLP) IS A PHYSIOLOGISequence details | THE PROTEIN BEARS AN N-TERMINAL HEXA-HISTIDINE PURIFICATI | |
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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: 2.31 Å3/Da / Density % sol: 42.42 % / Description: NONE |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: VAPOUR DIFFUSION, HANGING DROP, 293K, 1 TO 1 MIXTURE OF RESERVOIR TO PROTEIN SOLUTION. RESERVOIR CONTAINED 1.8 M AMMONIUM SULFATE, 10 % W/V PEG400, 0.1 M MES PH 6.5. PROTEIN SOLUTION ...Details: VAPOUR DIFFUSION, HANGING DROP, 293K, 1 TO 1 MIXTURE OF RESERVOIR TO PROTEIN SOLUTION. RESERVOIR CONTAINED 1.8 M AMMONIUM SULFATE, 10 % W/V PEG400, 0.1 M MES PH 6.5. PROTEIN SOLUTION CONTAINED PABC PROTEIN AT 33 MG/ML, 500 MM NACL, 100 MM HEPES PH 7.5, 0.1 MM PYRIDOXAL PHOSPHATE AND 10 MM PARA-AMINOBENZOIC ACID. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.977 |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 13, 2010 |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.977 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→30 Å / Num. obs: 56255 / % possible obs: 98.9 % / Observed criterion σ(I): 2 / Redundancy: 3.7 % / Biso Wilson estimate: 18.4 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 10.7 |
Reflection shell | Resolution: 1.75→5.53 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 2.5 / % possible all: 98.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1ET0 Resolution: 1.75→101.34 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.937 / SU B: 2.162 / SU ML: 0.07 / Cross valid method: THROUGHOUT / ESU R: 0.116 / ESU R Free: 0.118 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY. THE SIDE-CHAIN FOR ARG 90 IN BOTH CHAIN A AND CHAIN B HAS ZERO OCCUPANCY BEYOND CB. THE PRESENCE OF THIS ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY. THE SIDE-CHAIN FOR ARG 90 IN BOTH CHAIN A AND CHAIN B HAS ZERO OCCUPANCY BEYOND CB. THE PRESENCE OF THIS ARGININE IN THE PROTEIN SEQUENCE HAS BEEN CONFIRMED BY DNA SEQUENCING.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.669 Å2
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Refinement step | Cycle: LAST / Resolution: 1.75→101.34 Å
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Refine LS restraints |
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