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Open data
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Basic information
Entry | Database: PDB / ID: 2vus | ||||||
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Title | Crystal structure of unliganded 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 / DNA-binding transcription factor activity, RNA polymerase II-specific / oxidoreductase activity / 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 | ![]() | 602.4 KB | Display | ![]() |
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PDB format | ![]() | 498.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 566.1 KB | Display | ![]() |
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Full document | ![]() | 653.4 KB | Display | |
Data in XML | ![]() | 126 KB | Display | |
Data in CIF | ![]() | 175.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2vutC ![]() 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.) ![]() ![]() Plasmid: PET3A / Production host: ![]() ![]() |
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-Non-polymers , 4 types, 1635 molecules 






#3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-CL / #5: Chemical | ChemComp-ZN / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.11 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: 0.9765 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→30 Å / Num. obs: 132091 / % possible obs: 98.8 % / Observed criterion σ(I): -1 / Redundancy: 4 % / Biso Wilson estimate: 33.3 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 8.4 |
Reflection shell | Resolution: 2.6→2.69 Å / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 1.5 / % possible all: 97.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRIES 1K6J AND 4GAT Resolution: 2.6→29.97 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 5805574.65 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: BULK SOLVENT MODEL USED A SELF PATTERSON FUNCTION SHOWED A SIGNIFICANT PEAK INDICATIVE OF PSEUDO-TRANSLATION
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 36.3595 Å2 / ksol: 0.3 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 30.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.6→29.97 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.76 Å / Rfactor Rfree error: 0.011 / Total num. of bins used: 6
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Xplor file |
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