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Open data
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Basic information
| Entry | Database: PDB / ID: 2vut | ||||||
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| Title | Crystal structure of NAD-bound NmrA-AreA zinc finger complex | ||||||
Components |
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Keywords | TRANSCRIPTION / TRANSCRIPTION REGULATION / PROTEIN-PROTEIN INTERACTIONS / METAL-BINDING / NITRATE ASSIMILATION / ZINC-FINGER / DNA-BINDING / ZINC FINGERS / ZINC / AREA / NMRA / NUCLEUS / ACTIVATOR / GATA-TYPE | ||||||
| Function / homology | Function and homology informationnitrogen catabolite repression of transcription from RNA polymerase II promoter / regulation of amide catabolic process / nitrogen catabolite repression of transcription / : / regulation of nitrogen utilization / NADP+ binding / NAD+ binding / nitrate assimilation / NAD binding / regulation of gene expression ...nitrogen catabolite repression of transcription from RNA polymerase II promoter / regulation of amide catabolic process / nitrogen catabolite repression of transcription / : / regulation of nitrogen utilization / NADP+ binding / NAD+ binding / nitrate assimilation / NAD binding / regulation of gene expression / sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / oxidoreductase activity / RNA polymerase II cis-regulatory region sequence-specific DNA binding / chromatin remodeling / negative regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Kotaka, M. / Johnson, C. / Lamb, H.K. / Hawkins, A.R. / Ren, J. / Stammers, D.K. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2008Title: Structural Analysis of the Recognition of the Negative Regulator Nmra and DNA by the Zinc Finger from the Gata-Type Transcription Factor Area. Authors: Kotaka, M. / Johnson, C. / Lamb, H.K. / Hawkins, A.R. / Ren, J. / Stammers, D.K. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 2vut.cif.gz | 622.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2vut.ent.gz | 517.2 KB | Display | PDB format |
| PDBx/mmJSON format | 2vut.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2vut_validation.pdf.gz | 2.8 MB | Display | wwPDB validaton report |
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| Full document | 2vut_full_validation.pdf.gz | 2.9 MB | Display | |
| Data in XML | 2vut_validation.xml.gz | 133.5 KB | Display | |
| Data in CIF | 2vut_validation.cif.gz | 180.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vu/2vut ftp://data.pdbj.org/pub/pdb/validation_reports/vu/2vut | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 2vusC ![]() 2vuuC ![]() 1k6jS ![]() 4gatS C: citing same article ( S: Starting model for refinement |
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| Similar structure data |
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Links
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Assembly
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Components
-Protein / Protein/peptide , 2 types, 16 molecules ABCDEFGHIJKLMNOP
| #1: Protein | Mass: 38835.238 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Plasmid: PET / Production host: ![]() #2: Protein/peptide | Mass: 4789.604 Da / Num. of mol.: 8 / Fragment: ZINC FINGER DOMAIN, RESIDUES 670-712 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Non-polymers , 5 types, 1983 molecules 








| #3: Chemical | ChemComp-NAD / #4: Chemical | ChemComp-CL / #5: Chemical | #6: Chemical | ChemComp-ZN / #7: 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: 3.1 Å3/Da / Density % sol: 60 % / Description: NONE |
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| Crystal grow | pH: 6.4 Details: 0.2M LI2SO4, 0.1M BIS-TRIS PH 6.4, 15% - 17% PEG3350 |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 |
| Detector | Type: ADSC CCD / Detector: CCD |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
| Reflection | Resolution: 2.3→30 Å / Num. obs: 180785 / % possible obs: 94.8 % / Observed criterion σ(I): -1 / Redundancy: 6 % / Biso Wilson estimate: 22.6 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 12.7 |
| Reflection shell | Resolution: 2.3→2.38 Å / Rmerge(I) obs: 0.44 / Mean I/σ(I) obs: 1.6 / % possible all: 71.3 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRIES 1K6J AND 4GAT Resolution: 2.3→29.86 Å / Rfactor Rfree error: 0.002 / Data cutoff high absF: 2465599.64 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: A SELF PATTERSON FUNCTION SHOWED A SIGNIFICANT PEAK INDICATIVE OF PSEUDO-TRANSLATION.
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| Solvent computation | Solvent model: FLAT MODEL / Bsol: 56.8585 Å2 / ksol: 0.35 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 35.5 Å2
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| Refine analyze |
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| Refinement step | Cycle: LAST / Resolution: 2.3→29.86 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 2.3→2.44 Å / Rfactor Rfree error: 0.007 / Total num. of bins used: 6
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| Xplor file |
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