+Open data
-Basic information
Entry | Database: PDB / ID: 3p87 | ||||||
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Title | Structure of human PCNA bound to RNASEH2B PIP box peptide | ||||||
Components |
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Keywords | HYDROLASE/DNA BINDING PROTEIN / DNA binding / DNA replication / DNA repair / sliding clamp / PCNA Peptide Interacting Peptide (PIP) motif / PIP-box motif / DNA clamp / processivity factor / RNase H2 / FEN-1 / Ligase / polymerases / helicases / nucleases / nucleus / HYDROLASE-DNA BINDING PROTEIN complex | ||||||
Function / homology | Function and homology information ribonucleotide metabolic process / ribonuclease H2 complex / positive regulation of deoxyribonuclease activity / dinucleotide insertion or deletion binding / PCNA-p21 complex / mitotic telomere maintenance via semi-conservative replication / purine-specific mismatch base pair DNA N-glycosylase activity / positive regulation of DNA-directed DNA polymerase activity / MutLalpha complex binding / nuclear lamina ...ribonucleotide metabolic process / ribonuclease H2 complex / positive regulation of deoxyribonuclease activity / dinucleotide insertion or deletion binding / PCNA-p21 complex / mitotic telomere maintenance via semi-conservative replication / purine-specific mismatch base pair DNA N-glycosylase activity / positive regulation of DNA-directed DNA polymerase activity / MutLalpha complex binding / nuclear lamina / Polymerase switching / Telomere C-strand (Lagging Strand) Synthesis / Processive synthesis on the lagging strand / PCNA complex / Processive synthesis on the C-strand of the telomere / Removal of the Flap Intermediate / regulation of DNA damage checkpoint / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Polymerase switching on the C-strand of the telomere / Transcription of E2F targets under negative control by DREAM complex / Removal of the Flap Intermediate from the C-strand / replisome / RNA catabolic process / response to L-glutamate / histone acetyltransferase binding / leading strand elongation / DNA polymerase processivity factor activity / replication fork processing / G1/S-Specific Transcription / response to dexamethasone / nuclear replication fork / SUMOylation of DNA replication proteins / estrous cycle / PCNA-Dependent Long Patch Base Excision Repair / mismatch repair / cyclin-dependent protein kinase holoenzyme complex / translesion synthesis / response to cadmium ion / DNA polymerase binding / base-excision repair, gap-filling / positive regulation of DNA repair / epithelial cell differentiation / regulation of G2/M transition of mitotic cell cycle / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / replication fork / positive regulation of DNA replication / male germ cell nucleus / liver regeneration / nuclear estrogen receptor binding / Recognition of DNA damage by PCNA-containing replication complex / Termination of translesion DNA synthesis / Translesion Synthesis by POLH / HDR through Homologous Recombination (HRR) / Dual Incision in GG-NER / receptor tyrosine kinase binding / cellular response to hydrogen peroxide / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / cellular response to UV / positive regulation of fibroblast proliferation / cellular response to xenobiotic stimulus / response to estradiol / E3 ubiquitin ligases ubiquitinate target proteins / gene expression / heart development / fibroblast proliferation / in utero embryonic development / damaged DNA binding / chromosome, telomeric region / nuclear body / negative regulation of gene expression / centrosome / chromatin binding / chromatin / protein-containing complex binding / negative regulation of transcription by RNA polymerase II / enzyme binding / extracellular exosome / nucleoplasm / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.99 Å | ||||||
Authors | Bubeck, D. / Reijns, M.A. / Graham, S.C. / Astell, K.R. / Jones, E.Y. / Jackson, A.P. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2011 Title: PCNA directs type 2 RNase H activity on DNA replication and repair substrates. Authors: Bubeck, D. / Reijns, M.A. / Graham, S.C. / Astell, K.R. / Jones, E.Y. / Jackson, A.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3p87.cif.gz | 291.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3p87.ent.gz | 236.7 KB | Display | PDB format |
PDBx/mmJSON format | 3p87.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p8/3p87 ftp://data.pdbj.org/pub/pdb/validation_reports/p8/3p87 | HTTPS FTP |
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-Related structure data
Related structure data | 3p83C 1axcS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 28795.752 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PCNA / Plasmid: pT7.7 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P12004 #2: Protein/peptide | Mass: 2563.088 Da / Num. of mol.: 6 / Fragment: UNP RESIDUES 290-306 / Mutation: RNASEH2B:290-312 / Source method: obtained synthetically Details: This sequence occurs naturally in humans. It correspond to residues 290-312 of RNASEH2B Source: (synth.) Homo sapiens (human) / References: UniProt: Q5TBB1 |
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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: 2.15 Å3/Da / Density % sol: 42.78 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 3.5 Details: 3M NaCl, 0.1M citrate, pH 3.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.982 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 23, 2009 |
Radiation | Monochromator: double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.982 Å / Relative weight: 1 |
Reflection | Resolution: 2.99→47.5 Å / Num. all: 31807 / Num. obs: 31807 / % possible obs: 99.9 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 3.7 % / Biso Wilson estimate: 68.32 Å2 / Rmerge(I) obs: 0.126 / Net I/σ(I): 8 |
Reflection shell | Resolution: 2.99→3.09 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.852 / Mean I/σ(I) obs: 1.8 / Num. unique all: 2930 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1AXC Resolution: 2.99→47.45 Å / Cor.coef. Fo:Fc: 0.9354 / Cor.coef. Fo:Fc free: 0.9265 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 72.18 Å2
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Refine analyze | Luzzati coordinate error obs: 0.511 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.99→47.45 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.99→3.09 Å / Total num. of bins used: 16
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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