+Open data
-Basic information
Entry | Database: PDB / ID: 6tdn | ||||||
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Title | Bam_5925cDD 5924nDD docking domains | ||||||
Components | Beta-ketoacyl synthase,Beta-ketoacyl synthase | ||||||
Keywords | PROTEIN BINDING / docking domain / polyketide synthase | ||||||
Function / homology | Function and homology information N-acetyltransferase activity / phosphopantetheine binding / 3-oxoacyl-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process Similarity search - Function | ||||||
Biological species | Burkholderia ambifaria AMMD (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Risser, F. / Chagot, B. | ||||||
Funding support | France, 1items
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Citation | Journal: J.Struct.Biol. / Year: 2020 Title: Towards improved understanding of intersubunit interactions in modular polyketide biosynthesis: Docking in the enacyloxin IIa polyketide synthase. Authors: Risser, F. / Collin, S. / Dos Santos-Morais, R. / Gruez, A. / Chagot, B. / Weissman, K.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6tdn.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb6tdn.ent.gz | 1 MB | Display | PDB format |
PDBx/mmJSON format | 6tdn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/td/6tdn ftp://data.pdbj.org/pub/pdb/validation_reports/td/6tdn | HTTPS FTP |
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-Related structure data
Related structure data | 6tddC 6tdmC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 9150.089 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Burkholderia ambifaria AMMD (bacteria) / Gene: Bamb_5925, Bamb_5924 / Plasmid: pBG102 / Production host: Escherichia coli (E. coli) / References: UniProt: Q0B303, UniProt: Q0B304 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Type: solution Contents: 1 mM [U-100% 13C; U-100% 15N] protein, 90% H2O/10% D2O Label: 13C_15N_sample / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1 mM / Component: protein / Isotopic labeling: [U-100% 13C; U-100% 15N] |
Sample conditions | Ionic strength: 0.1 M / Label: conditions_1 / pH: 6.5 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: fewest violations | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 25 |