[English] 日本語
![](img/lk-miru.gif)
- PDB-1lbg: LACTOSE OPERON REPRESSOR BOUND TO 21-BASE PAIR SYMMETRIC OPERATOR... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1lbg | ||||||
---|---|---|---|---|---|---|---|
Title | LACTOSE OPERON REPRESSOR BOUND TO 21-BASE PAIR SYMMETRIC OPERATOR DNA, ALPHA CARBONS ONLY | ||||||
![]() |
| ||||||
![]() | TRANSCRIPTION/DNA / TRANSCRIPTION REGULATION / DNA-BINDING / REPRESSOR / TRANSCRIPTION-DNA COMPLEX | ||||||
Function / homology | ![]() DNA-binding transcription repressor activity / cis-regulatory region sequence-specific DNA binding / transcription cis-regulatory region binding / DNA-binding transcription factor activity / negative regulation of DNA-templated transcription / regulation of DNA-templated transcription / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Lewis, M. / Chang, G. / Horton, N.C. / Kercher, M.A. / Pace, H.C. / Lu, P. | ||||||
![]() | ![]() Title: Crystal structure of the lactose operon repressor and its complexes with DNA and inducer. Authors: Lewis, M. / Chang, G. / Horton, N.C. / Kercher, M.A. / Pace, H.C. / Schumacher, M.A. / Brennan, R.G. / Lu, P. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 108.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 59.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 352.1 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 474.7 KB | Display | |
Data in XML | ![]() | 15.7 KB | Display | |
Data in CIF | ![]() | 34.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: DNA chain | Mass: 6462.196 Da / Num. of mol.: 4 / Source method: obtained synthetically #2: Protein | Mass: 38657.051 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.6 Å3/Da / Density % sol: 65.5 % | |||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal | *PLUS Density % sol: 65.5 % | |||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / pH: 8.5 / Method: macro seeding | |||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Detector | Type: SIEMENS / Detector: AREA DETECTOR |
---|---|
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 11283 / % possible obs: 90 % / Rmerge(I) obs: 0.058 |
Reflection | *PLUS Highest resolution: 4.8 Å / Lowest resolution: 15 Å / % possible obs: 90 % / Num. measured all: 43976 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 4.8→15 Å / Rfactor Rwork: 0.26 / Rfactor obs: 0.26 / σ(F): 0 Details: GENERATED SYMMETRY MOLECULES YIELD CLOSE CONTACTS IN CRYSTAL PACKING. THIS IS PARTICULARLY TRUE FOR ATOMS OF LAC RESIDUES 351 AND 350 OF CHAIN D WHICH CONFLICT WITH END BASE G IN CHAIN G. ...Details: GENERATED SYMMETRY MOLECULES YIELD CLOSE CONTACTS IN CRYSTAL PACKING. THIS IS PARTICULARLY TRUE FOR ATOMS OF LAC RESIDUES 351 AND 350 OF CHAIN D WHICH CONFLICT WITH END BASE G IN CHAIN G. THE ELECTRON DENSITY FOR THE ENDS OF THE DNA STRANDS IS WEAK. THE POSITION OF THE END BASE G IN DNA CHAIN G SHOULD BE USED WITH CAUTION. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 15 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 4.8→15 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 4.8 Å / Lowest resolution: 15 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |