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Open data
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Basic information
Entry | Database: PDB / ID: 6iid | ||||||
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Title | Human EXOG-H140A in complex with RNA-DNA chimeric duplex | ||||||
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![]() | HYDROLASE/DNA / Enzyme-substrate complex / Mitochondrial exonuclease / HYDROLASE-DNA complex / DNA BINDING PROTEIN | ||||||
Function / homology | ![]() Hydrolases; Acting on ester bonds; Endoribonucleases that are active with either ribo- or deoxyribonucleic acids and produce 5'-phosphomonoesters / single-stranded DNA endodeoxyribonuclease activity / apoptotic DNA fragmentation / Strand-asynchronous mitochondrial DNA replication / 5'-3' exonuclease activity / RNA endonuclease activity / endonuclease activity / nucleic acid binding / mitochondrial inner membrane / protein-containing complex ...Hydrolases; Acting on ester bonds; Endoribonucleases that are active with either ribo- or deoxyribonucleic acids and produce 5'-phosphomonoesters / single-stranded DNA endodeoxyribonuclease activity / apoptotic DNA fragmentation / Strand-asynchronous mitochondrial DNA replication / 5'-3' exonuclease activity / RNA endonuclease activity / endonuclease activity / nucleic acid binding / mitochondrial inner membrane / protein-containing complex / mitochondrion / metal ion binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() synthetic construct (others) | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Wu, C.C. / Lin, J.L.J. / Yuan, H.S. | ||||||
![]() | ![]() Title: A unique exonuclease ExoG cleaves between RNA and DNA in mitochondrial DNA replication. Authors: Wu, C.C. / Lin, J.L.J. / Yang-Yen, H.F. / Yuan, H.S. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 496.8 KB | Display | ![]() |
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PDB format | ![]() | 404.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5zkiSC ![]() 5zkjC S: Starting model for refinement C: citing same article ( |
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Similar 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
#1: Protein | Mass: 39216.262 Da / Num. of mol.: 4 / Mutation: H140A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9Y2C4, Hydrolases; Acting on ester bonds; Endoribonucleases that are active with either ribo- or deoxyribonucleic acids and produce 5'-phosphomonoesters #2: DNA/RNA hybrid | Mass: 3735.416 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) #3: DNA chain | Mass: 3623.368 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) #4: Chemical | ChemComp-MG / #5: Water | ChemComp-HOH / | Has protein modification | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.64 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop Details: 0.2 M magnesium formate dehydrate and 20% [w/v] PEG 3350 PH range: 6.6-7.2 |
-Data collection
Diffraction | Mean temperature: 80 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX300HE / Detector: CCD / Date: Aug 3, 2018 |
Radiation | Monochromator: LN2-Cooled, Fixed-Exit Double Crystal Monochromator Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.986→30 Å / Num. obs: 30771 / % possible obs: 96.7 % / Redundancy: 1.9 % / CC1/2: 0.941 / Rmerge(I) obs: 0.085 / Rpim(I) all: 0.085 / Rrim(I) all: 0.12 / Χ2: 0.999 / Net I/σ(I): 8.9 |
Reflection shell | Resolution: 3→3.08 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.432 / Mean I/σ(I) obs: 1.59 / Num. unique obs: 2246 / CC1/2: 0.855 / Rpim(I) all: 0.432 / Rrim(I) all: 0.611 / Χ2: 1.008 / % possible all: 91.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5ZKI Resolution: 2.986→29.834 Å / SU ML: 0.4 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 28.65
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.986→29.834 Å
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Refine LS restraints |
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LS refinement shell |
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