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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 | ||||||
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![]() | 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 | ![]() nitrogen catabolite repression of transcription from RNA polymerase II promoter / regulation of amide catabolic process / nitrogen catabolite repression of transcription / regulation of arginine metabolic process / 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 arginine metabolic process / regulation of nitrogen utilization / NADP+ binding / NAD+ binding / nitrate assimilation / NAD binding / regulation of gene expression / sequence-specific DNA binding / oxidoreductase activity / DNA-binding transcription factor activity, RNA polymerase II-specific / chromatin remodeling / RNA polymerase II cis-regulatory region sequence-specific DNA binding / 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 | ![]() ![]() ![]() | ||||||
![]() | Kotaka, M. / Johnson, C. / Lamb, H.K. / Hawkins, A.R. / Ren, J. / Stammers, D.K. | ||||||
![]() | ![]() Title: 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 622.7 KB | Display | ![]() |
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PDB format | ![]() | 517.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.8 MB | Display | ![]() |
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Full document | ![]() | 2.9 MB | Display | |
Data in XML | ![]() | 133.5 KB | Display | |
Data in CIF | ![]() | 180.4 KB | Display | |
Arichive directory | ![]() ![]() | 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 ![](data/chem/img/NAD.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/HOH.gif)
#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: ![]() |
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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: ![]() ![]() ![]() |
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: ![]() Starting 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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