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- PDB-1plq: CRYSTAL STRUCTURE OF THE EUKARYOTIC DNA POLYMERASE PROCESSIVITY F... -
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Basic information
Entry | Database: PDB / ID: 1plq | ||||||
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Title | CRYSTAL STRUCTURE OF THE EUKARYOTIC DNA POLYMERASE PROCESSIVITY FACTOR PCNA | ||||||
![]() | PROLIFERATING CELL NUCLEAR ANTIGEN (PCNA) | ||||||
![]() | DNA-BINDING / NUCLEAR PROTEIN / DNA REPLICATION / PROCESSIVITY FACTOR | ||||||
Function / homology | ![]() 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 / SUMOylation of DNA replication proteins / positive regulation of DNA metabolic process / maintenance of DNA trinucleotide repeats / Translesion Synthesis by POLH ...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 / SUMOylation of DNA replication proteins / positive regulation of DNA metabolic process / maintenance of DNA trinucleotide repeats / Translesion Synthesis by POLH / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / establishment of mitotic sister chromatid cohesion / PCNA complex / Termination of translesion DNA synthesis / lagging strand elongation / postreplication repair / 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 / subtelomeric heterochromatin formation / mismatch repair / translesion synthesis / positive regulation of DNA repair / replication fork / positive regulation of DNA replication / nucleotide-excision repair / mitotic cell cycle / chromosome, telomeric region / DNA binding / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Krishna, T.S.R. / Kong, X.-P. / Gary, S. / Burgers, P.M. / Kuriyan, J. | ||||||
![]() | ![]() Title: 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: ![]() Title: 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: ![]() Title: Sliding Clamps of DNA Polymerases Authors: Kuriyan, J. / Donnell, M. #3: ![]() Title: 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. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 65.6 KB | Display | ![]() |
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PDB format | ![]() | 48.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 413.9 KB | Display | ![]() |
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Full document | ![]() | 418.4 KB | Display | |
Data in XML | ![]() | 12.9 KB | Display | |
Data in CIF | ![]() | 17.6 KB | Display | |
Arichive directory | ![]() ![]() | 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: Chemical | #3: Water | ChemComp-HOH / | Compound details | THE STRUCTURE IS THAT OF THE MERCURY COMPLEX OF PCNA. | Nonpolymer details | THE STRUCTURE IS OF THE MERCURY COMPLEX OF THE PROTEIN INVOLVING TWO MERCURY ATOMS PER MONOMER. THE ...THE STRUCTURE IS OF THE MERCURY COMPLEX OF THE PROTEIN INVOLVING TWO MERCURY ATOMS PER MONOMER. THE FIRST MERCURY ATOM CROSSLINKS | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.13 Å3/Da / Density % sol: 76 % | ||||||||||||||||||||||||||||||||||||
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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: 26608 / % possible obs: 93.7 % / Observed criterion σ(I): 1 |
Reflection | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 30 Å / Redundancy: 11.3 % / Num. measured all: 300303 / Rmerge(I) obs: 0.089 |
Reflection shell | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 2.34 Å / % possible obs: 92.7 % |
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Processing
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Refinement | Resolution: 2.3→5 Å / σ(F): 2
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Displacement parameters | Biso mean: 34.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→5 Å
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Refine LS restraints |
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