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Yorodumi- PDB-6hpu: Crystal structure of human Pif1 helicase in complex with ADP-AlF4 -
+Open data
-Basic information
Entry | Database: PDB / ID: 6hpu | ||||||
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Title | Crystal structure of human Pif1 helicase in complex with ADP-AlF4 | ||||||
Components | ATP-dependent DNA helicase PIF1 | ||||||
Keywords | HYDROLASE / Pif1 / 5'-3' DNA helicase / Duplex Unwinding / Telomere Maintenance / DNA Repair | ||||||
Function / homology | Function and homology information 5'-3' DNA/RNA helicase activity / telomerase inhibitor activity / G-quadruplex DNA binding / mitochondrial genome maintenance / : / regulation of telomere maintenance / DNA duplex unwinding / single-stranded DNA helicase activity / telomeric DNA binding / negative regulation of telomere maintenance via telomerase ...5'-3' DNA/RNA helicase activity / telomerase inhibitor activity / G-quadruplex DNA binding / mitochondrial genome maintenance / : / regulation of telomere maintenance / DNA duplex unwinding / single-stranded DNA helicase activity / telomeric DNA binding / negative regulation of telomere maintenance via telomerase / Telomere Extension By Telomerase / telomere maintenance via telomerase / replication fork / 5'-3' DNA helicase activity / DNA recombination / DNA replication / DNA helicase / chromosome, telomeric region / DNA repair / magnesium ion binding / ATP hydrolysis activity / mitochondrion / nucleoplasm / ATP binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.96 Å | ||||||
Authors | Levdikov, V.M. / Dehghani-Tafti, S. / Bax, B.D. / Sanders, C.M. / Antson, A.A. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2019 Title: Structural and functional analysis of the nucleotide and DNA binding activities of the human PIF1 helicase. Authors: Dehghani-Tafti, S. / Levdikov, V. / Antson, A.A. / Bax, B. / Sanders, C.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6hpu.cif.gz | 176.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6hpu.ent.gz | 139.9 KB | Display | PDB format |
PDBx/mmJSON format | 6hpu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6hpu_validation.pdf.gz | 927.4 KB | Display | wwPDB validaton report |
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Full document | 6hpu_full_validation.pdf.gz | 953.6 KB | Display | |
Data in XML | 6hpu_validation.xml.gz | 33.5 KB | Display | |
Data in CIF | 6hpu_validation.cif.gz | 44.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hp/6hpu ftp://data.pdbj.org/pub/pdb/validation_reports/hp/6hpu | HTTPS FTP |
-Related structure data
Related structure data | 6hphSC 6hpqC 6hptC 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 45483.582 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: SRM - cloning artefact / Source: (gene. exp.) Homo sapiens (human) / Gene: PIF1, C15orf20 / Plasmid: pET / Details (production host): pET / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q9H611, DNA helicase #2: Chemical | #3: Chemical | #4: Chemical | |
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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: 5.51 Å3/Da / Density % sol: 77.68 % |
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Crystal grow | Temperature: 274 K / Method: vapor diffusion, sitting drop / Details: MES, Ca-acetate, PEG 20K, PEG550 MME / PH range: 6-8 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.92819 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Dec 12, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92819 Å / Relative weight: 1 |
Reflection | Resolution: 3.96→104.93 Å / Num. obs: 17663 / % possible obs: 100 % / Redundancy: 12.3 % / Biso Wilson estimate: 151.7 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.08 / Net I/σ(I): 17.1 |
Reflection shell | Resolution: 3.96→4.06 Å / Redundancy: 12.8 % / Rmerge(I) obs: 0.857 / Mean I/σ(I) obs: 2.9 / Num. unique obs: 1273 / CC1/2: 0.892 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6HPH Resolution: 3.96→91.03 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.926 / SU B: 37.623 / SU ML: 0.487 / Cross valid method: THROUGHOUT / ESU R Free: 0.638 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 151.675 Å2
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Refinement step | Cycle: 1 / Resolution: 3.96→91.03 Å
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