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Open data
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Basic information
Entry | Database: PDB / ID: 2pjr | ||||||
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Title | HELICASE PRODUCT COMPLEX | ||||||
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![]() | HYDROLASE/DNA / HELICASE PCRA / HYDROLASE / DNA / PRODUCT COMPLEX / HYDROLASE-DNA COMPLEX | ||||||
Function / homology | ![]() DNA helicase complex / DNA 3'-5' helicase / recombinational repair / DNA unwinding involved in DNA replication / 3'-5' DNA helicase activity / isomerase activity / ATP hydrolysis activity / DNA binding / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Velankar, S.S. / Soultanas, P. / Dillingham, M.S. / Subramanya, H.S. / Wigley, D.B. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 274.3 KB | Display | ![]() |
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PDB format | ![]() | 217.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 495.9 KB | Display | ![]() |
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Full document | ![]() | 593.3 KB | Display | |
Data in XML | ![]() | 56.5 KB | Display | |
Data in CIF | ![]() | 75.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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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.) ![]() ![]() Production host: ![]() ![]() 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.) ![]() ![]() Production host: ![]() ![]() References: UniProt: P56255, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides |
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-Non-polymers , 1 types, 2 molecules ![](data/chem/img/SO4.gif)
#6: Chemical |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: ![]() ![]() ![]() |
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 |
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Processing
Software | Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.9→15 Å
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Refine LS restraints |
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