+Open data
-Basic information
Entry | Database: PDB / ID: 5e0v | ||||||
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Title | Human PCNA variant (S228I) complexed with FEN1 at 2.1 Angstroms | ||||||
Components |
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Keywords | DNA BINDING PROTEIN / DNA replication / sliding clamp | ||||||
Function / homology | Function and homology information positive regulation of sister chromatid cohesion / flap endonuclease activity / telomere maintenance via semi-conservative replication / double-stranded DNA exodeoxyribonuclease activity / positive regulation of deoxyribonuclease activity / dinucleotide insertion or deletion binding / PCNA-p21 complex / mitotic telomere maintenance via semi-conservative replication / nucleic acid metabolic process / purine-specific mismatch base pair DNA N-glycosylase activity ...positive regulation of sister chromatid cohesion / flap endonuclease activity / telomere maintenance via semi-conservative replication / double-stranded DNA exodeoxyribonuclease activity / positive regulation of deoxyribonuclease activity / dinucleotide insertion or deletion binding / PCNA-p21 complex / mitotic telomere maintenance via semi-conservative replication / nucleic acid metabolic process / purine-specific mismatch base pair DNA N-glycosylase activity / 5'-flap endonuclease activity / nuclear lamina / MutLalpha complex binding / DNA replication, removal of RNA primer / positive regulation of DNA-directed DNA polymerase activity / Polymerase switching / Telomere C-strand (Lagging Strand) Synthesis / 5'-3' exonuclease activity / Processive synthesis on the lagging strand / UV protection / PCNA complex / Removal of the Flap Intermediate / Processive synthesis on the C-strand of the telomere / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Polymerase switching on the C-strand of the telomere / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Transcription of E2F targets under negative control by DREAM complex / Removal of the Flap Intermediate from the C-strand / HDR through MMEJ (alt-NHEJ) / replisome / exonuclease activity / response to L-glutamate / histone acetyltransferase binding / DNA polymerase processivity factor activity / G1/S-Specific Transcription / leading strand elongation / response to dexamethasone / replication fork processing / Early Phase of HIV Life Cycle / nuclear replication fork / SUMOylation of DNA replication proteins / POLB-Dependent Long Patch Base Excision Repair / estrous cycle / PCNA-Dependent Long Patch Base Excision Repair / cyclin-dependent protein kinase holoenzyme complex / mismatch repair / translesion synthesis / response to cadmium ion / DNA polymerase binding / epithelial cell differentiation / positive regulation of DNA repair / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / base-excision repair, gap-filling / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / positive regulation of DNA replication / replication fork / 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 / double-strand break repair via homologous recombination / base-excision repair / HDR through Homologous Recombination (HRR) / Dual Incision in GG-NER / receptor tyrosine kinase binding / memory / cellular response to hydrogen peroxide / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / cellular response to UV / double-strand break repair / RNA-DNA hybrid ribonuclease activity / cellular response to xenobiotic stimulus / E3 ubiquitin ligases ubiquitinate target proteins / response to estradiol / heart development / manganese ion binding / double-stranded DNA binding / endonuclease activity / DNA replication / chromosome, telomeric region / damaged DNA binding / Hydrolases; Acting on ester bonds / nuclear body / DNA repair / centrosome / chromatin binding / protein-containing complex binding / chromatin / nucleolus / enzyme binding / negative regulation of transcription by RNA polymerase II / magnesium ion binding / protein-containing complex / mitochondrion Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.074 Å | ||||||
Authors | Duffy, C.M. / Hilbert, B.J. / Kelch, B.A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2016 Title: A Disease-Causing Variant in PCNA Disrupts a Promiscuous Protein Binding Site. Authors: Duffy, C.M. / Hilbert, B.J. / Kelch, B.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5e0v.cif.gz | 198.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5e0v.ent.gz | 161.7 KB | Display | PDB format |
PDBx/mmJSON format | 5e0v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5e0v_validation.pdf.gz | 444.6 KB | Display | wwPDB validaton report |
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Full document | 5e0v_full_validation.pdf.gz | 448.5 KB | Display | |
Data in XML | 5e0v_validation.xml.gz | 20.5 KB | Display | |
Data in CIF | 5e0v_validation.cif.gz | 28.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e0/5e0v ftp://data.pdbj.org/pub/pdb/validation_reports/e0/5e0v | HTTPS FTP |
-Related structure data
Related structure data | 5e0tC 5e0uC 1ul7S 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 28821.830 Da / Num. of mol.: 2 / Mutation: S228I Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PCNA / Plasmid: pET3c / Production host: Escherichia coli (E. coli) / Strain (production host): BLR(DE3) / References: UniProt: P12004 #2: Protein/peptide | Mass: 1772.954 Da / Num. of mol.: 2 / Fragment: UNP residues 299-314 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) References: UniProt: B4DWZ4, UniProt: P39748*PLUS, Hydrolases; Acting on ester bonds #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.05 Å3/Da / Density % sol: 39.88 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 2.35 M ammonium sulfate, 100 mM sodium acetate pH 4.6, 40% (v/v) -1,3-Butanediol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.033 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Mar 16, 2015 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.033 Å / Relative weight: 1 |
Reflection | Resolution: 2.074→30.95 Å / Num. obs: 29298 / % possible obs: 99.7 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.078 / Net I/σ(I): 16.68 |
Reflection shell | Resolution: 2.074→2.12 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.636 / Mean I/σ(I) obs: 2.1 / % possible all: 98.33 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1UL7 Resolution: 2.074→30.945 Å / Cross valid method: FREE R-VALUE / σ(F): 1.99 / Phase error: 37.63 / Stereochemistry target values: TWIN_LSQ_F
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.074→30.945 Å
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Refine LS restraints |
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LS refinement shell |
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