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Yorodumi- PDB-5m3k: A multi-component acyltransferase PhlABC from Pseudomonas protegens -
+Open data
-Basic information
Entry | Database: PDB / ID: 5m3k | ||||||
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Title | A multi-component acyltransferase PhlABC from Pseudomonas protegens | ||||||
Components |
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Keywords | TRANSFERASE / acyltransferase / Pseudomonas protegens / PhlABC / multi-component | ||||||
Function / homology | Function and homology information acyltransferase activity, transferring groups other than amino-acyl groups / 3-oxoacyl-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process Similarity search - Function | ||||||
Biological species | Pseudomonas fluorescens (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.83 Å | ||||||
Authors | Pavkov-Keller, T. / Schmidt, N.G. / Kroutil, W. / Gruber, K. | ||||||
Citation | Journal: Chembiochem / Year: 2019 Title: Structure and Catalytic Mechanism of a Bacterial Friedel-Crafts Acylase. Authors: Pavkov-Keller, T. / Schmidt, N.G. / Zadlo-Dobrowolska, A. / Kroutil, W. / Gruber, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5m3k.cif.gz | 669.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5m3k.ent.gz | 552.9 KB | Display | PDB format |
PDBx/mmJSON format | 5m3k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5m3k_validation.pdf.gz | 455.5 KB | Display | wwPDB validaton report |
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Full document | 5m3k_full_validation.pdf.gz | 460.3 KB | Display | |
Data in XML | 5m3k_validation.xml.gz | 61.6 KB | Display | |
Data in CIF | 5m3k_validation.cif.gz | 87.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m3/5m3k ftp://data.pdbj.org/pub/pdb/validation_reports/m3/5m3k | HTTPS FTP |
-Related structure data
Related structure data | 5mg5C 1tvzS 3zbgS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Refine code: _
NCS ensembles :
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-Components
#1: Protein | Mass: 38565.480 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas fluorescens (bacteria) / Gene: phlA / Production host: Escherichia coli (E. coli) / References: UniProt: Q9TP23 #2: Protein | Mass: 16666.434 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5) (bacteria) Strain: ATCC BAA-477 / NRRL B-23932 / Pf-5 / Gene: phlB, PFL_5956 / Production host: Escherichia coli (E. coli) / References: UniProt: Q4K419 #3: Protein | Mass: 42581.941 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: CYS:SCY issue - at the position 88 the Cystein residue is modified and has attached acetyl group (SCY) Source: (gene. exp.) Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5) (bacteria) Strain: ATCC BAA-477 / NRRL B-23932 / Pf-5 / Gene: phlC, PFL_5955 / Production host: Escherichia coli (E. coli) / References: UniProt: Q4K420 #4: Chemical | #5: Water | ChemComp-HOH / | |
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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: 4.35 Å3/Da / Density % sol: 71.7 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, sitting drop Details: 12 mg mL-1 protein solution Index screen crystallization condition #91 (0.15 M, DL-malic acid pH 7.0, 20% w/v polyethylene glycol 3,350) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.8726 Å |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Nov 19, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8726 Å / Relative weight: 1 |
Reflection | Resolution: 2.83→49.862 Å / Num. obs: 82036 / % possible obs: 100 % / Redundancy: 8.5 % / CC1/2: 0.98 / Rmerge(I) obs: 0.255 / Rrim(I) all: 0.271 / Net I/σ(I): 7.87 |
Reflection shell | Resolution: 2.83→2.94 Å / Redundancy: 8.5 % / Rmerge(I) obs: 0.891 / Mean I/σ(I) obs: 2.23 / CC1/2: 0.67 / Rrim(I) all: 0.271 / % possible all: 98 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1tvz, 3zbg Resolution: 2.83→49.862 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.927 / SU B: 20.171 / SU ML: 0.179 / Cross valid method: THROUGHOUT / ESU R: 0.386 / ESU R Free: 0.24 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.9 Å / Shrinkage radii: 0.9 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.211 Å2
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Refinement step | Cycle: 1 / Resolution: 2.83→49.862 Å
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Refine LS restraints |
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