+Open data
-Basic information
Entry | Database: PDB / ID: 2pjr | ||||||
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Title | HELICASE PRODUCT COMPLEX | ||||||
Components |
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Keywords | HYDROLASE/DNA / HELICASE PCRA / HYDROLASE / DNA / PRODUCT COMPLEX / HYDROLASE-DNA COMPLEX | ||||||
Function / homology | Function and homology information DNA 3'-5' helicase / DNA unwinding involved in DNA replication / isomerase activity / DNA helicase activity / ATP hydrolysis activity / DNA binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | Geobacillus stearothermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å | ||||||
Authors | Velankar, S.S. / Soultanas, P. / Dillingham, M.S. / Subramanya, H.S. / Wigley, D.B. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1999 Title: Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Authors: Velankar, S.S. / Soultanas, P. / Dillingham, M.S. / Subramanya, H.S. / Wigley, D.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2pjr.cif.gz | 274.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2pjr.ent.gz | 217.1 KB | Display | PDB format |
PDBx/mmJSON format | 2pjr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pj/2pjr ftp://data.pdbj.org/pub/pdb/validation_reports/pj/2pjr | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-DNA chain , 3 types, 4 molecules CDHI
#1: DNA chain | Mass: 1476.007 Da / Num. of mol.: 2 / Source method: obtained synthetically #2: DNA chain | | Mass: 573.430 Da / Num. of mol.: 1 / Source method: obtained synthetically #3: DNA chain | | Mass: 1480.012 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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-PROTEIN (HELICASE ... , 2 types, 4 molecules AFBG
#4: Protein | Mass: 63369.156 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-548 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Geobacillus stearothermophilus (bacteria) Production host: Escherichia coli (E. coli) References: UniProt: P56255, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides #5: Protein | Mass: 10713.169 Da / Num. of mol.: 2 / Fragment: RESIDUES 556-650 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Geobacillus stearothermophilus (bacteria) Production host: Escherichia coli (E. coli) References: UniProt: P56255, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides |
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-Non-polymers , 1 types, 2 molecules
#6: 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: 2.45 Å3/Da / Density % sol: 49.8 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.5 / Details: pH 8.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging dropDetails: drop consists of 1:1 mixture of well and protein solutions | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.9 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→10 Å / Num. all: 31850 / Num. obs: 31850 / % possible obs: 97.9 % / Observed criterion σ(I): 0 / Redundancy: 2 % / Rmerge(I) obs: 0.068 |
-Processing
Software | Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.9→15 Å / Rfactor Rfree error: 0.007 / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.9→15 Å
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Refine LS restraints |
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