[English] 日本語
![](img/lk-miru.gif)
- PDB-3fis: THE MOLECULAR STRUCTURE OF WILD-TYPE AND A MUTANT FIS PROTEIN: RE... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 3fis | ||||||
---|---|---|---|---|---|---|---|
Title | THE MOLECULAR STRUCTURE OF WILD-TYPE AND A MUTANT FIS PROTEIN: RELATIONSHIP BETWEEN MUTATIONAL CHANGES AND RECOMBINATIONAL ENHANCER FUNCTION OR DNA BINDING | ||||||
![]() | FACTOR FOR INVERSION STIMULATION (FIS) | ||||||
![]() | DNA BINDING PROTEIN / DNA-BINDING PROTEIN | ||||||
Function / homology | ![]() invertasome / positive regulation of DNA recombination / sequence-specific DNA binding, bending / provirus excision / nucleoid / DNA-binding transcription repressor activity / DNA-binding transcription activator activity / chromosome organization / core promoter sequence-specific DNA binding / protein-DNA complex ...invertasome / positive regulation of DNA recombination / sequence-specific DNA binding, bending / provirus excision / nucleoid / DNA-binding transcription repressor activity / DNA-binding transcription activator activity / chromosome organization / core promoter sequence-specific DNA binding / protein-DNA complex / response to radiation / nucleosome / sequence-specific DNA binding / transcription cis-regulatory region binding / DNA-templated transcription / regulation of DNA-templated transcription / protein homodimerization activity / DNA binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Yuan, H.S. / Finkel, S.E. / Feng, J-A. / Johnson, R.C. / Dickerson, R.E. | ||||||
![]() | ![]() Title: The molecular structure of wild-type and a mutant Fis protein: relationship between mutational changes and recombinational enhancer function or DNA binding. Authors: Yuan, H.S. / Finkel, S.E. / Feng, J.A. / Kaczor-Grzeskowiak, M. / Johnson, R.C. / Dickerson, R.E. | ||||||
History |
| ||||||
Remark 650 | HELIX THE EXTENDED REGIONS BEFORE A-HELIX (RESIDUES A 20 TO A 25 AND B 20 TO B 25) AND AFTER A- ...HELIX THE EXTENDED REGIONS BEFORE A-HELIX (RESIDUES A 20 TO A 25 AND B 20 TO B 25) AND AFTER A-HELIX (RESIDUES A 43 TO A 46 AND B 43 TO B 46) ARE MORE FLEXIBLE. THE STRUCTURE IN THESE REGIONS IS ILL-DEFINED AND THE ATOMS HAVE HIGH TEMPERATURE FACTORS. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 39.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 29 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.3 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 431.1 KB | Display | |
Data in XML | ![]() | 8.2 KB | Display | |
Data in CIF | ![]() | 10.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 11252.918 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.82 % | ||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 8.2 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Reflection | *PLUS Highest resolution: 2.25 Å / Num. obs: 6451 / % possible obs: 68 % / Num. measured all: 30267 / Rmerge(I) obs: 0.0323 |
---|
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor Rwork: 0.183 / Rfactor obs: 0.183 / Highest resolution: 2.3 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.3 Å
| ||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||
Refinement | *PLUS Lowest resolution: 8 Å / Num. reflection obs: 6053 / σ(F): 2 / Rfactor obs: 0.183 / Rfactor Rwork: 0.183 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
|