[English] 日本語
Yorodumi- PDB-6qu1: Crystal structure of the KAP1 RBCC domain in complex with the SMA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6qu1 | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of the KAP1 RBCC domain in complex with the SMARCAD1 CUE1 domain at 3.7 angstrom resolution. | ||||||
Components |
| ||||||
Keywords | LIGASE / TRIM28 / transcriptional co-repressor / CUE domain / Ubuiquitin | ||||||
Function / homology | Function and homology information : / : / convergent extension involved in axis elongation / negative regulation of DNA demethylation / Krueppel-associated box domain binding / chromosome separation / embryonic placenta morphogenesis / positive regulation of DNA methylation-dependent heterochromatin formation / suppression of viral release by host / regulation of DNA recombination ...: / : / convergent extension involved in axis elongation / negative regulation of DNA demethylation / Krueppel-associated box domain binding / chromosome separation / embryonic placenta morphogenesis / positive regulation of DNA methylation-dependent heterochromatin formation / suppression of viral release by host / regulation of DNA recombination / epigenetic programming of gene expression / DNA double-strand break processing / negative regulation of single stranded viral RNA replication via double stranded DNA intermediate / genomic imprinting / chromo shadow domain binding / Generic Transcription Pathway / ATP-dependent chromatin remodeler activity / SUMO transferase activity / nuclear replication fork / protein sumoylation / epithelial to mesenchymal transition / ATP-dependent activity, acting on DNA / heterochromatin / embryo implantation / positive regulation of DNA repair / SUMOylation of transcription cofactors / ubiquitin binding / helicase activity / promoter-specific chromatin binding / euchromatin / RING-type E3 ubiquitin transferase / HCMV Early Events / positive regulation of protein import into nucleus / RNA polymerase II transcription regulator complex / ubiquitin-protein transferase activity / transcription corepressor activity / ubiquitin protein ligase activity / site of double-strand break / chromatin organization / DNA helicase / transcription coactivator activity / protein kinase activity / chromatin remodeling / DNA repair / innate immune response / negative regulation of DNA-templated transcription / chromatin binding / ubiquitin protein ligase binding / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / ATP hydrolysis activity / protein-containing complex / DNA binding / RNA binding / zinc ion binding / nucleoplasm / ATP binding / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.7 Å | ||||||
Authors | Newman, J.A. / Aitkenhead, H. / Gavard, A. / Lim, M. / Williams, H.L. / Svejstrup, J.Q. / von Delft, F. / Arrowsmith, C.H. / Edwards, A. / Bountra, C. / Gileadi, O. | ||||||
Funding support | United Kingdom, 1items
| ||||||
Citation | Journal: Structure / Year: 2019 Title: A Ubiquitin-Binding Domain that Binds a Structural Fold Distinct from that of Ubiquitin. Authors: Lim, M. / Newman, J.A. / Williams, H.L. / Masino, L. / Aitkenhead, H. / Gravard, A.E. / Gileadi, O. / Svejstrup, J.Q. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 6qu1.cif.gz | 78 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb6qu1.ent.gz | 56 KB | Display | PDB format |
PDBx/mmJSON format | 6qu1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qu/6qu1 ftp://data.pdbj.org/pub/pdb/validation_reports/qu/6qu1 | HTTPS FTP |
---|
-Related structure data
Related structure data | 6h3aSC S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 35985.312 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: The protein is a construct with an internal deletion of residues 141-202,The protein is a construct with an internal deletion of residues 141-202,The protein is a construct with an internal ...Details: The protein is a construct with an internal deletion of residues 141-202,The protein is a construct with an internal deletion of residues 141-202,The protein is a construct with an internal deletion of residues 141-202,The protein is a construct with an internal deletion of residues 141-202,The protein is a construct with an internal deletion of residues 141-202,The protein is a construct with an internal deletion of residues 141-202 Source: (gene. exp.) Homo sapiens (human) / Gene: TRIM28, KAP1, RNF96, TIF1B / Production host: Escherichia coli (E. coli) References: UniProt: Q13263, RING-type E3 ubiquitin transferase |
---|---|
#2: Protein/peptide | Mass: 5343.150 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCAD1, KIAA1122 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9H4L7, DNA helicase |
#3: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 4.18 Å3/Da / Density % sol: 70.54 % |
---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 25 % PEG 3350, 0.1 M HEPES pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.92 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Oct 5, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 3.7→29.431 Å / Num. obs: 7157 / % possible obs: 99.7 % / Redundancy: 9.2 % / CC1/2: 0.995 / Rmerge(I) obs: 0.235 / Rpim(I) all: 0.106 / Net I/σ(I): 7.3 |
Reflection shell | Resolution: 3.7→4.14 Å / Redundancy: 7.3 % / Rmerge(I) obs: 2.081 / Mean I/σ(I) obs: 1.4 / Num. unique obs: 1948 / CC1/2: 0.816 / Rpim(I) all: 0.805 / % possible all: 99.4 |
-Processing
Software |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6H3A Resolution: 3.7→29.431 Å / Cross valid method: FREE R-VALUE / σ(F): 0.23
| ||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.7→29.431 Å
| ||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||
LS refinement shell | Resolution: 3.7→3.895 Å
|