+Open data
-Basic information
Entry | Database: PDB / ID: 5anr | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of a human 4E-T - DDX6 - CNOT1 complex | ||||||
Components |
| ||||||
Keywords | RNA BINDING PROTEIN | ||||||
Function / homology | Function and homology information negative regulation of deadenylation-dependent decapping of nuclear-transcribed mRNA / positive regulation of cytoplasmic mRNA processing body assembly / CCR4-NOT core complex / CCR4-NOT complex / armadillo repeat domain binding / regulation of stem cell population maintenance / negative regulation of retinoic acid receptor signaling pathway / positive regulation of mRNA catabolic process / mRNA decay by 5' to 3' exoribonuclease / negative regulation of intracellular estrogen receptor signaling pathway ...negative regulation of deadenylation-dependent decapping of nuclear-transcribed mRNA / positive regulation of cytoplasmic mRNA processing body assembly / CCR4-NOT core complex / CCR4-NOT complex / armadillo repeat domain binding / regulation of stem cell population maintenance / negative regulation of retinoic acid receptor signaling pathway / positive regulation of mRNA catabolic process / mRNA decay by 5' to 3' exoribonuclease / negative regulation of intracellular estrogen receptor signaling pathway / nuclear-transcribed mRNA poly(A) tail shortening / trophectodermal cell differentiation / nuclear export signal receptor activity / miRNA-mediated post-transcriptional gene silencing / viral RNA genome packaging / Deadenylation of mRNA / miRNA-mediated gene silencing by inhibition of translation / nuclear retinoic acid receptor binding / M-decay: degradation of maternal mRNAs by maternally stored factors / P-body assembly / RISC complex / mRNA stabilization / peroxisomal membrane / TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain / positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / stem cell population maintenance / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / negative regulation of neuron differentiation / stress granule assembly / nuclear estrogen receptor binding / helicase activity / P-body / PML body / neuron differentiation / kinase binding / cytoplasmic ribonucleoprotein granule / cytoplasmic stress granule / protein import into nucleus / molecular adaptor activity / RNA helicase activity / negative regulation of translation / RNA helicase / nuclear speck / cadherin binding / translation / protein domain specific binding / intracellular membrane-bounded organelle / mRNA binding / negative regulation of transcription by RNA polymerase II / ATP hydrolysis activity / RNA binding / extracellular space / ATP binding / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.102 Å | ||||||
Authors | Basquin, J. / Oezguer, S. / Conti, E. | ||||||
Citation | Journal: Cell Rep. / Year: 2015 Title: Structure of a Human 4E-T/Ddx6/Cnot1 Complex Reveals the Different Interplay of Ddx6-Binding Proteins with the Ccr4-not Complex. Authors: Ozgur, S. / Basquin, J. / Kamenska, A. / Filipowicz, W. / Standart, N. / Conti, E. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 5anr.cif.gz | 142.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb5anr.ent.gz | 109.4 KB | Display | PDB format |
PDBx/mmJSON format | 5anr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5anr_validation.pdf.gz | 444.3 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 5anr_full_validation.pdf.gz | 448.5 KB | Display | |
Data in XML | 5anr_validation.xml.gz | 25.9 KB | Display | |
Data in CIF | 5anr_validation.cif.gz | 37.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/an/5anr ftp://data.pdbj.org/pub/pdb/validation_reports/an/5anr | HTTPS FTP |
-Related structure data
Related structure data | 4ct4S S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
| ||||||||
Components on special symmetry positions |
|
-Components
#1: Protein | Mass: 29695.352 Da / Num. of mol.: 1 / Fragment: MIF4G DOMAIN, UNP RESIDUES 1063-1314 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PEC_HIS_SUMO / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): GOLD / References: UniProt: A5YKK6 |
---|---|
#2: Protein | Mass: 43189.195 Da / Num. of mol.: 1 / Fragment: RECA1 AND RECA2, UNP RESIDUES 95-469 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PEC_HIS_SUMO / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): GOLD / References: UniProt: P26196, RNA helicase |
#3: Protein/peptide | Mass: 5092.398 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 199-239 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PEC_HIS_SUMO / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): GOLD / References: UniProt: Q9NRA8 |
#4: Water | ChemComp-HOH / |
Sequence details | CHAIN A: QGPDSM IS COMING FROM THE CLEAVAGE SITE CHAIN B: RSM IS COMING FROM THE CLEAVAGE SITE ...CHAIN A: QGPDSM IS COMING FROM THE CLEAVAGE SITE CHAIN B: RSM IS COMING FROM THE CLEAVAGE SITE CHAIN C: RSM IS COMING FROM THE CLEAVAGE SITE |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 47.01 % / Description: NONE |
---|---|
Crystal grow | pH: 8 / Details: 50 MM TRIS PH 8.0, 35% MPD |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Oct 26, 2014 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→47.32 Å / Num. obs: 51910 / % possible obs: 99.7 % / Observed criterion σ(I): 1.6 / Redundancy: 9.4 % / Biso Wilson estimate: 37.8 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 17.61 |
Reflection shell | Resolution: 2.1→2.18 Å / Redundancy: 7 % / Rmerge(I) obs: 1.04 / Mean I/σ(I) obs: 1.6 / % possible all: 97.4 |
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 4CT4 Resolution: 2.102→47.324 Å / SU ML: 0.25 / σ(F): 1.05 / Phase error: 26.12 / Stereochemistry target values: ML
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.102→47.324 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|