[English] 日本語
Yorodumi- PDB-3i7n: Crystal Structure of DDB1 in Complex with the H-Box Motif of WDTC1 -
+Open data
-Basic information
Entry | Database: PDB / ID: 3i7n | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal Structure of DDB1 in Complex with the H-Box Motif of WDTC1 | ||||||
Components |
| ||||||
Keywords | PROTEIN BINDING / DDB1 / WDTC1 / DCAF9 / H-Box Motif / Cytoplasm / DNA damage / DNA repair / DNA-binding / Host-virus interaction / Nucleus / Phosphoprotein / Polymorphism / Ubl conjugation / Ubl conjugation pathway / Alternative splicing / TPR repeat / WD repeat | ||||||
Function / homology | Function and homology information intracellular chemical homeostasis / negative regulation of fatty acid biosynthetic process / positive regulation by virus of viral protein levels in host cell / epigenetic programming in the zygotic pronuclei / spindle assembly involved in female meiosis / Cul4-RING E3 ubiquitin ligase complex / UV-damage excision repair / enzyme inhibitor activity / biological process involved in interaction with symbiont / WD40-repeat domain binding ...intracellular chemical homeostasis / negative regulation of fatty acid biosynthetic process / positive regulation by virus of viral protein levels in host cell / epigenetic programming in the zygotic pronuclei / spindle assembly involved in female meiosis / Cul4-RING E3 ubiquitin ligase complex / UV-damage excision repair / enzyme inhibitor activity / biological process involved in interaction with symbiont / WD40-repeat domain binding / regulation of mitotic cell cycle phase transition / Cul4A-RING E3 ubiquitin ligase complex / Cul4B-RING E3 ubiquitin ligase complex / ubiquitin ligase complex scaffold activity / regulation of cell size / negative regulation of reproductive process / negative regulation of developmental process / cullin family protein binding / viral release from host cell / ectopic germ cell programmed cell death / proteasomal protein catabolic process / positive regulation of viral genome replication / positive regulation of gluconeogenesis / post-translational protein modification / nucleotide-excision repair / Recognition of DNA damage by PCNA-containing replication complex / DNA Damage Recognition in GG-NER / multicellular organism growth / regulation of circadian rhythm / Dual Incision in GG-NER / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / Wnt signaling pathway / Formation of Incision Complex in GG-NER / histone deacetylase binding / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / positive regulation of protein catabolic process / cellular response to insulin stimulus / glucose metabolic process / cellular response to UV / rhythmic process / protein-macromolecule adaptor activity / Neddylation / site of double-strand break / histone binding / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / in utero embryonic development / chromosome, telomeric region / damaged DNA binding / protein ubiquitination / DNA repair / apoptotic process / DNA damage response / protein-containing complex binding / nucleolus / negative regulation of apoptotic process / negative regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / extracellular space / extracellular exosome / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Li, T. / Robert, E.I. / Breugel, P.C.V. / Strubin, M. / Zheng, N. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2010 Title: A promiscuous alpha-helical motif anchors viral hijackers and substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery. Authors: Li, T. / Robert, E.I. / van Breugel, P.C. / Strubin, M. / Zheng, N. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 3i7n.cif.gz | 214.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb3i7n.ent.gz | 170.3 KB | Display | PDB format |
PDBx/mmJSON format | 3i7n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3i7n_validation.pdf.gz | 442.9 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 3i7n_full_validation.pdf.gz | 511.2 KB | Display | |
Data in XML | 3i7n_validation.xml.gz | 47.4 KB | Display | |
Data in CIF | 3i7n_validation.cif.gz | 63.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i7/3i7n ftp://data.pdbj.org/pub/pdb/validation_reports/i7/3i7n | HTTPS FTP |
-Related structure data
Related structure data | 3i7hC 3i7kC 3i7lC 3i7oC 3i7pC 3i89C 3i8cC 3i8eC 2b5mS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 127399.766 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DDB1, XAP1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q16531 |
---|---|
#2: Protein/peptide | Mass: 1658.945 Da / Num. of mol.: 1 / Fragment: Residue 5-17 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q8N5D0 |
Sequence details | MUTATIONS OCCURRED DURING THE CLONING OF DDB1 |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.02 Å3/Da / Density % sol: 59.31 % |
---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 16% PEG 4000, 0.2M SODIUM CHLORIDE, 0.1M MES, 0.005M DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 173 K | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1.0,1.005 | |||||||||
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: May 28, 2008 | |||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
| |||||||||
Reflection | Resolution: 2.8→48.68 Å / Num. all: 39494 / Num. obs: 36206 / % possible obs: 91.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 7.2 % / Rmerge(I) obs: 0.067 / Net I/σ(I): 28.5 | |||||||||
Reflection shell | Resolution: 2.8→2.87 Å / Rmerge(I) obs: 0.565 / Mean I/σ(I) obs: 2.7 / Num. unique all: 2433 / % possible all: 97.3 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2B5M Resolution: 2.8→48.68 Å / Cor.coef. Fo:Fc: 0.904 / Cor.coef. Fo:Fc free: 0.874 / SU B: 17.332 / SU ML: 0.34 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R: 0.692 / ESU R Free: 0.414 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 71.58 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→48.68 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.8→2.873 Å / Total num. of bins used: 20
|