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- PDB-1xxa: C-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR/ L-ARGIN... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1xxa | ||||||
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Title | C-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR/ L-ARGININE COMPLEX; PB DERIVATIVE | ||||||
![]() | ARGININE REPRESSOR | ||||||
![]() | COMPLEX (DNA BINDING PROTEIN/PEPTIDE) / COMPLEX (DNA BINDING PROTEIN-PEPTIDE) / COMPLEX (DNA BINDING PROTEIN-PEPTIDE) complex | ||||||
Function / homology | ![]() regulation of arginine biosynthetic process / regulation of arginine catabolic process / plasmid recombination / negative regulation of DNA-templated transcription initiation / positive regulation of DNA-templated transcription initiation / arginine biosynthetic process / arginine binding / cis-regulatory region sequence-specific DNA binding / protein complex oligomerization / transcription regulator complex ...regulation of arginine biosynthetic process / regulation of arginine catabolic process / plasmid recombination / negative regulation of DNA-templated transcription initiation / positive regulation of DNA-templated transcription initiation / arginine biosynthetic process / arginine binding / cis-regulatory region sequence-specific DNA binding / protein complex oligomerization / transcription regulator complex / DNA-binding transcription factor activity / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Van Duyne, G.D. / Ghosh, G. / Maas, W.K. / Sigler, P.B. | ||||||
![]() | ![]() Title: Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli. Authors: Van Duyne, G.D. / Ghosh, G. / Maas, W.K. / Sigler, P.B. #1: ![]() Title: The Arginine Repressor of Escherichia Coli Authors: Maas, W.K. #2: ![]() Title: Nucleotide Sequence of the Argr Gene of Escherichia Coli K-12 and Isolation of its Product, the Arginine Repressor Authors: Lim, D.B. / Oppenheim, J.D. / Eckhardt, T. / Maas, W.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 | ![]() | 103.7 KB | Display | ![]() |
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PDB format | ![]() | 80.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 416.6 KB | Display | ![]() |
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Full document | ![]() | 430.1 KB | Display | |
Data in XML | ![]() | 11.3 KB | Display | |
Data in CIF | ![]() | 19.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 8351.467 Da / Num. of mol.: 6 / Fragment: INITIATOR MET PLUS C-TERMINAL RESIDUES 80 - 156 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-ARG / #3: Chemical | ChemComp-PB / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.43 Å3/Da / Density % sol: 49.3 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 18 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: FUJI / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→50 Å / Num. obs: 24878 / % possible obs: 95 % / Observed criterion σ(I): -3 / Redundancy: 6.2 % / Rmerge(I) obs: 0.089 |
Reflection | *PLUS Rmerge(I) obs: 0.089 |
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Processing
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Refinement | Resolution: 2.2→8 Å / σ(F): 3 /
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Displacement parameters | Biso mean: 42 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.35 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 23025 / Num. reflection obs: 19076 / Rfactor all: 0.241 / Rfactor obs: 0.195 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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