+Open data
-Basic information
Entry | Database: PDB / ID: 1w5f | ||||||
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Title | FtsZ, T7 mutated, domain swapped (T. maritima) | ||||||
Components | CELL DIVISION PROTEIN FTSZ | ||||||
Keywords | CELL DIVISION / CELL-DIVISION PROTEIN / GTP-BINDING / MULTIGENE FAMILY / SEPTATION / TUBULIN / FTSZ / FILAMENT / Z-RING / GTPASE / DOMAIN SWAPPED | ||||||
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 | THERMOTOGA MARITIMA (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 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 | 1w5f.cif.gz | 142.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1w5f.ent.gz | 110.1 KB | Display | PDB format |
PDBx/mmJSON format | 1w5f.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1w5f_validation.pdf.gz | 452.5 KB | Display | wwPDB validaton report |
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Full document | 1w5f_full_validation.pdf.gz | 465.3 KB | Display | |
Data in XML | 1w5f_validation.xml.gz | 28.1 KB | Display | |
Data in CIF | 1w5f_validation.cif.gz | 40.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w5/1w5f ftp://data.pdbj.org/pub/pdb/validation_reports/w5/1w5f | HTTPS FTP |
-Related structure data
Related structure data | 1w58C 1w59C 1w5aC 1w5bC 1w5eC 1fszS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 38673.426 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Details: RESIDUES 217-225 (INLD..FADIE) HAVE BEEN REPLACED WITH IRLTSRFARIE Source: (gene. exp.) THERMOTOGA MARITIMA (bacteria) / Plasmid: PHIS17 / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): C41 / References: UniProt: O08398 #2: Chemical | #3: Chemical | #4: 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 | Sequence details | RESIDUES 217-225 OF THE UNIPROT REFERENCE GIVEN BELOW (INLD..FADIE) HAVE BEEN REPLACED WITH: ...RESIDUES 217-225 OF THE UNIPROT REFERENCE GIVEN BELOW (INLD..FADIE) HAVE BEEN REPLACED WITH: IRLTSRFARI | |
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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: 2.39 Å3/Da / Density % sol: 49 % |
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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: 2→50 Å / Num. obs: 48484 / % possible obs: 99.5 % / Observed criterion σ(I): 0 / Redundancy: 4 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 15.4 |
Reflection shell | Resolution: 2→2.11 Å / Redundancy: 99.5 % / Rmerge(I) obs: 0.22 / Mean I/σ(I) obs: 5.7 / % possible all: 99.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1FSZ Resolution: 2→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: 51.1013 Å2 / ksol: 0.321584 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.01 Å / Total num. of bins used: 50 /
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Xplor file |
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