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Open data
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Basic information
Entry | Database: PDB / ID: 6cx4 | |||||||||
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Title | V180A Mutant of Yeast PCNA | |||||||||
![]() | Proliferating cell nuclear antigen | |||||||||
![]() | DNA BINDING PROTEIN / DNA Replication / DNA Repair / DNA Recombination Scaffold | |||||||||
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 | ![]() ![]() ![]() | |||||||||
![]() | Powers, K.T. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Identification of New Mutations at the PCNA Subunit Interface that Block Translesion Synthesis. Authors: Kondratick, C.M. / Boehm, E.M. / Dieckman, L.M. / Powers, K.T. / Sanchez, J.C. / Mueting, S.R. / Washington, M.T. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 62.7 KB | Display | ![]() |
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PDB format | ![]() | 45.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 421.4 KB | Display | ![]() |
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Full document | ![]() | 424.3 KB | Display | |
Data in XML | ![]() | 10.9 KB | Display | |
Data in CIF | ![]() | 13.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6cx2C ![]() 6cx3C ![]() 1plqS S: Starting model for refinement C: citing same article ( |
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Similar 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: 29054.145 Da / Num. of mol.: 1 / Mutation: V180A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: POL30, YBR088C, YBR0811 / Variant: S288c / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.37 Å3/Da / Density % sol: 77.09 % / Description: Regular Cube |
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Crystal grow | Temperature: 290.15 K / Method: vapor diffusion, hanging drop Details: 2.2M Ammonium Sulfate 0.2M Potassium Chloride 20% Glycerol |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: NOIR-1 / Detector: CCD / Date: Mar 15, 2013 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: Rosenbaum-Rock Si(111) saggitally focused mirrors Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 3.08→24.51 Å / Num. obs: 11585 / % possible obs: 100 % / Redundancy: 8.56 % / Rmerge(I) obs: 0.108 / Rrim(I) all: 0.116 / Χ2: 1.16 / Net I/σ(I): 9.3 / Num. measured all: 99880 / Scaling rejects: 750 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1PLQ Resolution: 3.081→24.51 Å / SU ML: 0.48 / Cross valid method: THROUGHOUT / σ(F): 0.77 / Phase error: 33.01
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||
Displacement parameters | Biso max: 231.39 Å2 / Biso mean: 153.7623 Å2 / Biso min: 113.02 Å2 | |||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 3.081→24.51 Å
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