+Open data
-Basic information
Entry | Database: PDB / ID: 4ou0 | ||||||
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Title | Crystal Structure of RPA32C | ||||||
Components | Replication protein A 32 kDa subunitDNA replication | ||||||
Keywords | DNA BINDING PROTEIN / winged-helix turn helix / protein-protein interaction / S-Methyl-Thio-Cysteine | ||||||
Function / homology | Function and homology information protein localization to chromosome / DNA replication factor A complex / regulation of DNA damage checkpoint / Removal of the Flap Intermediate / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Removal of the Flap Intermediate from the C-strand / G-rich strand telomeric DNA binding / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 ...protein localization to chromosome / DNA replication factor A complex / regulation of DNA damage checkpoint / Removal of the Flap Intermediate / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Removal of the Flap Intermediate from the C-strand / G-rich strand telomeric DNA binding / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 / regulation of double-strand break repair via homologous recombination / telomeric DNA binding / Presynaptic phase of homologous DNA pairing and strand exchange / PCNA-Dependent Long Patch Base Excision Repair / Activation of the pre-replicative complex / HSF1 activation / Regulation of HSF1-mediated heat shock response / mismatch repair / Activation of ATR in response to replication stress / mitotic G1 DNA damage checkpoint signaling / telomere maintenance / Translesion synthesis by REV1 / Translesion synthesis by POLK / Gap-filling DNA repair synthesis and ligation in GG-NER / Translesion synthesis by POLI / nucleotide-excision repair / Recognition of DNA damage by PCNA-containing replication complex / Fanconi Anemia Pathway / Termination of translesion DNA synthesis / double-strand break repair via homologous recombination / Translesion Synthesis by POLH / base-excision repair / HDR through Homologous Recombination (HRR) / G2/M DNA damage checkpoint / Dual Incision in GG-NER / PML body / Meiotic recombination / Formation of Incision Complex in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / single-stranded DNA binding / Processing of DNA double-strand break ends / protein phosphatase binding / Regulation of TP53 Activity through Phosphorylation / DNA replication / chromosome, telomeric region / damaged DNA binding / nuclear body / ubiquitin protein ligase binding / chromatin / enzyme binding / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.4 Å | ||||||
Authors | Feldkamp, M.D. / Mason, A.C. / Eichman, B.F. / Chazin, W.J. | ||||||
Citation | Journal: Biochemistry / Year: 2014 Title: Structural Analysis of Replication Protein A Recruitment of the DNA Damage Response Protein SMARCAL1. Authors: Feldkamp, M.D. / Mason, A.C. / Eichman, B.F. / Chazin, W.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4ou0.cif.gz | 51.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4ou0.ent.gz | 37.2 KB | Display | PDB format |
PDBx/mmJSON format | 4ou0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ou/4ou0 ftp://data.pdbj.org/pub/pdb/validation_reports/ou/4ou0 | HTTPS FTP |
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-Related structure data
Related structure data | 1dpuS S: Starting model for refinement |
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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: Protein | Mass: 7995.881 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 202-270 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: REPA2, RFA2, RPA2, RPA32, RPA34 / Production host: Escherichia coli (E. coli) / Strain (production host): BL-21 DE3 / References: UniProt: P15927 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 40.24 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, sitting drop / pH: 4.5 Details: 50 mM Sodium Acetate, 20% PEG 3350, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97857 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Feb 18, 2013 |
Radiation | Monochromator: C(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97857 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→30 Å / Num. obs: 12921 / % possible obs: 98.41 % / Redundancy: 7.6 % / Biso Wilson estimate: 35.4 Å2 / Rmerge(I) obs: 0.077 / Net I/σ(I): 14.46 |
Reflection shell | Resolution: 1.4→1.45 Å / Redundancy: 6.1 % / Rmerge(I) obs: 0.357 / Mean I/σ(I) obs: 4.51 / Num. unique all: 1161 / % possible all: 89.03 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1DPU Resolution: 1.4→30 Å / SU ML: 0.12 / σ(F): 1.38 / Phase error: 30.93 / 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 | |||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.4→30 Å
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Refine LS restraints |
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LS refinement shell |
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