+Open data
-Basic information
Entry | Database: PDB / ID: 7cd5 | ||||||
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Title | mAPE1-blunt-ended dsDNA product complex | ||||||
Components |
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Keywords | HYDROLASE/DNA / APE1 / protein-nucleic acid interaction / exonuclease / DNA repair / DNA BINDING PROTEIN / HYDROLASE-DNA complex | ||||||
Function / homology | Function and homology information Resolution of Abasic Sites (AP sites) / Resolution of AP sites via the multiple-nucleotide patch replacement pathway / Abasic sugar-phosphate removal via the single-nucleotide replacement pathway / PCNA-Dependent Long Patch Base Excision Repair / : / POLB-Dependent Long Patch Base Excision Repair / Displacement of DNA glycosylase by APEX1 / class II DNA-(apurinic or apyrimidinic site) endonuclease activity / phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands / telomere maintenance via base-excision repair ...Resolution of Abasic Sites (AP sites) / Resolution of AP sites via the multiple-nucleotide patch replacement pathway / Abasic sugar-phosphate removal via the single-nucleotide replacement pathway / PCNA-Dependent Long Patch Base Excision Repair / : / POLB-Dependent Long Patch Base Excision Repair / Displacement of DNA glycosylase by APEX1 / class II DNA-(apurinic or apyrimidinic site) endonuclease activity / phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands / telomere maintenance via base-excision repair / site-specific endodeoxyribonuclease activity, specific for altered base / negative regulation of smooth muscle cell migration / DNA-(abasic site) binding / : / double-stranded DNA exodeoxyribonuclease activity / double-stranded telomeric DNA binding / exodeoxyribonuclease III / double-stranded DNA 3'-5' DNA exonuclease activity / 3'-5'-DNA exonuclease activity / phosphoric diester hydrolase activity / DNA demethylation / cellular response to peptide hormone stimulus / NF-kappaB binding / positive regulation of G1/S transition of mitotic cell cycle / cellular response to cAMP / RNA endonuclease activity / DNA-(apurinic or apyrimidinic site) endonuclease activity / 3'-5' exonuclease activity / regulation of mRNA stability / telomere maintenance / cell redox homeostasis / base-excision repair / chromatin DNA binding / cellular response to hydrogen peroxide / regulation of apoptotic process / DNA recombination / transcription regulator complex / damaged DNA binding / transcription coactivator activity / oxidoreductase activity / nuclear speck / response to xenobiotic stimulus / DNA repair / centrosome / protein-containing complex binding / nucleolus / perinuclear region of cytoplasm / endoplasmic reticulum / positive regulation of transcription by RNA polymerase II / mitochondrion / DNA binding / RNA binding / nucleoplasm / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) synthetic construct (others) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Liu, T.C. / Hsiao, Y.Y. | ||||||
Funding support | Taiwan, 1items
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Citation | Journal: Nat Commun / Year: 2021 Title: APE1 distinguishes DNA substrates in exonucleolytic cleavage by induced space-filling. Authors: Liu, T.C. / Lin, C.T. / Chang, K.C. / Guo, K.W. / Wang, S. / Chu, J.W. / Hsiao, Y.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7cd5.cif.gz | 138.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7cd5.ent.gz | 103.3 KB | Display | PDB format |
PDBx/mmJSON format | 7cd5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cd/7cd5 ftp://data.pdbj.org/pub/pdb/validation_reports/cd/7cd5 | HTTPS FTP |
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-Related structure data
Related structure data | 7cd6C 1hd7S 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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1 |
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Unit cell |
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-Components
#1: DNA chain | Mass: 2739.824 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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#2: Protein | Mass: 39095.336 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Apex1, Ape, Apex, Ref1 / Production host: Escherichia coli (E. coli) References: UniProt: P28352, Hydrolases; Acting on ester bonds |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 4.58 Å3/Da / Density % sol: 73.12 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.1M Bis-Tris pH 6.5, 25% v/v Polyethylene glycol 300 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: NSRRC / Beamline: BL13C1 / Wavelength: 0.97622 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Feb 23, 2017 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97622 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.7→30 Å / Num. obs: 22366 / % possible obs: 99.5 % / Redundancy: 19.3 % / Rmerge(I) obs: 0.091 / Rpim(I) all: 0.02 / Rrim(I) all: 0.093 / Χ2: 1.112 / Net I/σ(I): 8.4 / Num. measured all: 431037 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1HD7 Resolution: 2.7→29.892 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.44 / Phase error: 22.44 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 151 Å2 / Biso mean: 65.2002 Å2 / Biso min: 32.07 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.7→29.892 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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Refinement TLS params. | Method: refined / Origin x: 49.5976 Å / Origin y: -21.7264 Å / Origin z: -0.389 Å
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Refinement TLS group |
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