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Yorodumi- PDB-5z4f: An anthrahydroquino-Gama-pyrone synthase Txn09 complexed with SUM -
+Open data
-Basic information
Entry | Database: PDB / ID: 5z4f | ||||||
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Title | An anthrahydroquino-Gama-pyrone synthase Txn09 complexed with SUM | ||||||
Components | TxnO9 | ||||||
Keywords | BIOSYNTHETIC PROTEIN / type II polyketide heterocyclase / enzyme mechanism / natural product / Streptomyces bottropensis | ||||||
Function / homology | Activator of Hsp90 ATPase homologue 1-like / Activator of Hsp90 ATPase homolog 1-like protein / START-like domain superfamily / Chem-96F / TxnO9 Function and homology information | ||||||
Biological species | Streptomyces bottropensis (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Song, Y.J. / Cao, C.Y. | ||||||
Citation | Journal: Angew. Chem. Int. Ed. Engl. / Year: 2018 Title: Enzymology of Anthraquinone-gamma-Pyrone Ring Formation in Complex Aromatic Polyketide Biosynthesis. Authors: Hou, X.F. / Song, Y.J. / Zhang, M. / Lan, W.X. / Meng, S. / Wang, C.X. / Pan, H.X. / Cao, C.Y. / Tang, G.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5z4f.cif.gz | 955.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5z4f.ent.gz | 801 KB | Display | PDB format |
PDBx/mmJSON format | 5z4f.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5z4f_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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Full document | 5z4f_full_validation.pdf.gz | 13.2 MB | Display | |
Data in XML | 5z4f_validation.xml.gz | 1009.3 KB | Display | |
Data in CIF | 5z4f_validation.cif.gz | 1.2 MB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z4/5z4f ftp://data.pdbj.org/pub/pdb/validation_reports/z4/5z4f | HTTPS FTP |
-Related structure data
Related structure data | 5z36C 5z4eC 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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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 17837.941 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces bottropensis (bacteria) / Production host: Escherichia coli K-12 (bacteria) / Strain (production host): K-12 / References: UniProt: A0A0K1H313 |
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#2: Chemical | ChemComp-96F / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Type: solution Contents: 0.7 mM [U-99% 13C; U-99% 15N] Txn09, 50 mM sodium chloride, 20 mM sodium phosphate, 10 % v/v Deuteration DMSO, 90% H2O/10% D2O Details: 10%DMSO / Label: 15N,13C_sample / Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 60 mM / Label: condition-1 / pH: 7.4 / Pressure: 1 atm / Temperature: 293 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |