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Yorodumi- PDB-1f4s: STRUCTURE OF TRANSCRIPTIONAL FACTOR ALCR IN COMPLEX WITH A TARGET DNA -
+Open data
-Basic information
Entry | Database: PDB / ID: 1f4s | ||||||
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Title | STRUCTURE OF TRANSCRIPTIONAL FACTOR ALCR IN COMPLEX WITH A TARGET DNA | ||||||
Components |
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Keywords | TRANSCRIPTION/DNA / PROTEIN-DNA COMPLEX / ZINC BINUCLEAR CLUSTER PROTEIN / TRANSCRIPTION-DNA COMPLEX | ||||||
Function / homology | Function and homology information acetaldehyde catabolic process / threonine catabolic process / ethanol catabolic process / DNA-binding transcription factor activity, RNA polymerase II-specific / chromatin remodeling / DNA-binding transcription factor activity / positive regulation of transcription by RNA polymerase II / DNA binding / zinc ion binding / nucleus Similarity search - Function | ||||||
Biological species | Emericella nidulans (mold) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing | ||||||
Authors | Cahuzac, B. / Cerdan, R. / Felenbok, B. / Guittet, E. | ||||||
Citation | Journal: Structure / Year: 2001 Title: The solution structure of an AlcR-DNA complex sheds light onto the unique tight and monomeric DNA binding of a Zn(2)Cys(6) protein. Authors: Cahuzac, B. / Cerdan, R. / Felenbok, B. / Guittet, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1f4s.cif.gz | 330.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1f4s.ent.gz | 283.1 KB | Display | PDB format |
PDBx/mmJSON format | 1f4s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f4/1f4s ftp://data.pdbj.org/pub/pdb/validation_reports/f4/1f4s | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: DNA chain | Mass: 3061.003 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: ALCR CONSENSUS HALF-TARGET | ||
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#2: DNA chain | Mass: 3029.993 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: ALCR CONSENSUS HALF-TARGET | ||
#3: Protein | Mass: 7580.351 Da / Num. of mol.: 1 / Mutation: N-TERMINAL DNA-BINDING DOMAIN, RESIDUES 1-60 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Emericella nidulans (mold) / Production host: Escherichia coli (E. coli) / References: UniProt: P21228 | ||
#4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1 mM AlcR U-15N, 1.1 mM double stranded DNA Solvent system: 20 mM phosphate buffer; 90%H2O, 10%D2O; pH 5.9 |
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Sample conditions | pH: 5.9 / Pressure: 1 atm / Temperature: 293 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing / Software ordinal: 1 Details: 1142 noe-derived constraints, 76 h-bond constraints, 33 phi angle restraints, 118 loose angle restraints on the DNA backbone | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: The submitted conformer models are the 10 structures with the lowest energy. Conformers calculated total number: 20 / Conformers submitted total number: 10 |