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Yorodumi- PDB-1plr: CRYSTAL STRUCTURE OF THE EUKARYOTIC DNA POLYMERASE PROCESSIVITY F... -
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Basic information
| Entry | Database: PDB / ID: 1plr | ||||||
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| Title | CRYSTAL STRUCTURE OF THE EUKARYOTIC DNA POLYMERASE PROCESSIVITY FACTOR PCNA | ||||||
Components | PROLIFERATING CELL NUCLEAR ANTIGEN (PCNA) | ||||||
Keywords | DNA-BINDING / NUCLEAR PROTEIN / DNA REPLICATION | ||||||
| Function / homology | Function and homology informationpositive regulation of DNA metabolic process / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / meiotic mismatch repair / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / E3 ubiquitin ligases ubiquitinate target proteins / Polymerase switching / maintenance of DNA trinucleotide repeats / SUMOylation of DNA replication proteins / Translesion synthesis by REV1 ...positive regulation of DNA metabolic process / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / meiotic mismatch repair / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / E3 ubiquitin ligases ubiquitinate target proteins / Polymerase switching / maintenance of DNA trinucleotide repeats / SUMOylation of DNA replication proteins / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / Translesion Synthesis by POLH / establishment of mitotic sister chromatid cohesion / PCNA complex / Termination of translesion DNA synthesis / lagging strand elongation / DNA damage tolerance / silent mating-type cassette heterochromatin formation / mitotic sister chromatid cohesion / error-free translesion synthesis / DNA polymerase processivity factor activity / leading strand elongation / Dual incision in TC-NER / translesion synthesis / subtelomeric heterochromatin formation / mismatch repair / positive regulation of DNA repair / positive regulation of DNA replication / replication fork / nucleotide-excision repair / mitotic cell cycle / chromosome, telomeric region / DNA binding / identical protein binding / nucleus Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / Resolution: 3 Å | ||||||
Authors | Krishna, T.S.R. / Kong, X.-P. / Gary, S. / Burgers, P.M. / Kuriyan, J. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1994Title: Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Authors: Krishna, T.S. / Kong, X.P. / Gary, S. / Burgers, P.M. / Kuriyan, J. #1: Journal: J.Mol.Biol. / Year: 1994Title: Crystallization of Proliferating Cell Nuclear Antigen (PCNA) from Saccharomyces Cerevisiae Authors: Krishna, T.S.R. / Kong, X.-P. / Gary, S. / Burgers, P. / Kuriyan, J. #2: Journal: J.Mol.Biol. / Year: 1993Title: Sliding Clamps of DNA Polymerases Authors: Kuriyan, J. / Donnell, M. #3: Journal: Cell(Cambridge,Mass.) / Year: 1992Title: Three-Dimensional Structure of the Beta Subunit of E. Coli DNA Polymerase III Holoenzyme: A Sliding DNA Clamp Authors: Kong, X.-P. / Onrust, R. / Donnell, M. / Kuriyan, J. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1plr.cif.gz | 61.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1plr.ent.gz | 45.8 KB | Display | PDB format |
| PDBx/mmJSON format | 1plr.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1plr_validation.pdf.gz | 416.9 KB | Display | wwPDB validaton report |
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| Full document | 1plr_full_validation.pdf.gz | 427.1 KB | Display | |
| Data in XML | 1plr_validation.xml.gz | 12.6 KB | Display | |
| Data in CIF | 1plr_validation.cif.gz | 16 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pl/1plr ftp://data.pdbj.org/pub/pdb/validation_reports/pl/1plr | HTTPS FTP |
-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 28944.051 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: P15873 |
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| #2: Water | ChemComp-HOH / |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 5.19 Å3/Da / Density % sol: 76.3 % | ||||||||||||||||||||||||||||||||||||
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| Crystal grow | *PLUS pH: 7.5 / Method: unknown / Details: Krishna, T.S.R., (1994) J.Mol.Biol., 241, 265. | ||||||||||||||||||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Radiation | Scattering type: x-ray |
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| Radiation wavelength | Relative weight: 1 |
| Reflection | Num. obs: 12273 / % possible obs: 86.3 % / Observed criterion σ(I): 1 |
| Reflection | *PLUS Highest resolution: 3 Å / Lowest resolution: 30 Å / Redundancy: 7.8 % / Num. measured all: 95433 / Rmerge(I) obs: 0.065 |
| Reflection shell | *PLUS Highest resolution: 3 Å / Lowest resolution: 3.05 Å / % possible obs: 80.9 % |
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Processing
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| Refinement | Resolution: 3→6 Å / σ(F): 2 /
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| Displacement parameters | Biso mean: 32 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3→6 Å
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| Refine LS restraints |
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