+Open data
-Basic information
Entry | Database: PDB / ID: 1w5e | ||||||
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Title | FtsZ W319Y mutant, P1 (M. jannaschii) | ||||||
Components | FTSZ | ||||||
Keywords | CELL DIVISION / CELL-DIVISION PROTEIN / GTP-BINDING / MULTIGENE FAMILY / SEPTATION / TUBULIN / FTSZ / FILAMENT / Z-RING / GTPASE | ||||||
Function / homology | Function and homology information FtsZ-dependent cytokinesis / division septum assembly / cell division site / protein polymerization / cell division / GTPase activity / GTP binding / cytoplasm Similarity search - Function | ||||||
Biological species | METHANOCALDOCOCCUS JANNASCHII (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Oliva, M.A. / Cordell, S.C. / Lowe, J. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2004 Title: Structural Insights Into Ftsz Protofilament Formation Authors: Oliva, M.A. / Cordell, S.C. / Lowe, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1w5e.cif.gz | 565.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1w5e.ent.gz | 467.4 KB | Display | PDB format |
PDBx/mmJSON format | 1w5e.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w5/1w5e ftp://data.pdbj.org/pub/pdb/validation_reports/w5/1w5e | HTTPS FTP |
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-Related structure data
Related structure data | 1w58C 1w59C 1w5aC 1w5bC 1w5fC 1fszS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
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Unit cell |
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-Components
#1: Protein | Mass: 38947.086 Da / Num. of mol.: 9 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) METHANOCALDOCOCCUS JANNASCHII (archaea) Plasmid: PHIS17 / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): C41 / References: UniProt: Q57816 #2: Chemical | ChemComp-GTP / #3: Water | ChemComp-HOH / | Compound details | THIS PROTEIN IS ESSENTIAL TO THE CELL-DIVISION PROCESS. IT SEEMS TO ASSEMBLE INTO A DYNAMIC RING ON ...THIS PROTEIN IS ESSENTIAL TO THE CELL-DIVISION PROCESS. IT SEEMS TO ASSEMBLE INTO A DYNAMIC RING ON THE INNER SURFACE OF THE CYTOPLASMI | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.71 Å3/Da / Density % sol: 68 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.93 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93 Å / Relative weight: 1 |
Reflection | Resolution: 3→50 Å / Num. obs: 85869 / % possible obs: 94.7 % / Observed criterion σ(I): 0 / Redundancy: 1.9 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 6.6 |
Reflection shell | Resolution: 3→3.16 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 1.9 / % possible all: 94.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1FSZ Resolution: 3→50 Å / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MLF
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Solvent computation | Bsol: 32.5513 Å2 / ksol: 0.273406 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 3→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3→3.02 Å / Total num. of bins used: 50 /
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Xplor file |
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