+Open data
-Basic information
Entry | Database: PDB / ID: 2ius | ||||||
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Title | E. coli FtsK motor domain | ||||||
Components | DNA TRANSLOCASE FTSK | ||||||
Keywords | MEMBRANE PROTEIN / NUCLEOTIDE-BINDING / CHROMOSOME PARTITION / ATP-BINDING / DNA-BINDING / CELL DIVISION / TRANSMEMBRANE / INNER MEMBRANE / HEXAMERIC RING / DNA TRANSLOCATION / KOPS / MEMBRANE / DIVISOME / CELL CYCLE / AAA ATPASE | ||||||
Function / homology | Function and homology information double-stranded DNA helicase activity / divisome complex / septum digestion after cytokinesis / DNA translocase activity / FtsZ-dependent cytokinesis / division septum assembly / response to osmotic stress / cellular response to antibiotic / cell division site / response to salt stress ...double-stranded DNA helicase activity / divisome complex / septum digestion after cytokinesis / DNA translocase activity / FtsZ-dependent cytokinesis / division septum assembly / response to osmotic stress / cellular response to antibiotic / cell division site / response to salt stress / chromosome segregation / sequence-specific DNA binding / cell division / positive regulation of DNA-templated transcription / ATP hydrolysis activity / DNA binding / ATP binding / membrane / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ESCHERICHIA COLI (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Massey, T.H. / Mercogliano, C.P. / Yates, J. / Sherratt, D.J. / Lowe, J. | ||||||
Citation | Journal: Mol.Cell / Year: 2006 Title: Double-Stranded DNA Translocation: Structure and Mechanism of Hexameric Ftsk Authors: Massey, T.H. / Mercogliano, C.P. / Yates, J. / Sherratt, D.J. / Lowe, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ius.cif.gz | 457.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ius.ent.gz | 377.7 KB | Display | PDB format |
PDBx/mmJSON format | 2ius.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/iu/2ius ftp://data.pdbj.org/pub/pdb/validation_reports/iu/2ius | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 56266.695 Da / Num. of mol.: 6 / Fragment: MOTOR DOMAIN, RESIDUES 818-1329 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P46889 #2: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, LYS 997 TO ALA ENGINEERED RESIDUE IN CHAIN B, LYS 997 TO ALA ...ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 51 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.979 |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→100 Å / Num. obs: 80156 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 58 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 11.3 |
Reflection shell | Resolution: 2.7→2.85 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.29 / Mean I/σ(I) obs: 3.9 / % possible all: 99.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.7→100 Å / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MLF
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Solvent computation | Bsol: 47.0167 Å2 / ksol: 0.350993 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 48 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→100 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.72 Å / Rfactor Rfree: 0.3746 / Rfactor Rwork: 0.3097 / Total num. of bins used: 50 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
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