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- PDB-4c0d: Structure of the NOT module of the human CCR4-NOT complex (CNOT1-... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4c0d | ||||||
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Title | Structure of the NOT module of the human CCR4-NOT complex (CNOT1-CNOT2-CNOT3) | ||||||
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![]() | GENE REGULATION / DEADENYLATION / MRNA DECAY / CCR4-NOT / HYDROLASE / TRANSCRIPTION | ||||||
Function / homology | ![]() positive regulation of cytoplasmic mRNA processing body assembly / CCR4-NOT core complex / armadillo repeat domain binding / CCR4-NOT complex / regulation of stem cell population maintenance / negative regulation of retinoic acid receptor signaling pathway / positive regulation of mRNA catabolic process / nuclear-transcribed mRNA poly(A) tail shortening / negative regulation of intracellular estrogen receptor signaling pathway / Deadenylation of mRNA ...positive regulation of cytoplasmic mRNA processing body assembly / CCR4-NOT core complex / armadillo repeat domain binding / CCR4-NOT complex / regulation of stem cell population maintenance / negative regulation of retinoic acid receptor signaling pathway / positive regulation of mRNA catabolic process / nuclear-transcribed mRNA poly(A) tail shortening / negative regulation of intracellular estrogen receptor signaling pathway / Deadenylation of mRNA / trophectodermal cell differentiation / miRNA-mediated post-transcriptional gene silencing / regulatory ncRNA-mediated gene silencing / M-decay: degradation of maternal mRNAs by maternally stored factors / nuclear retinoic acid receptor binding / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / peroxisomal membrane / positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / transcription corepressor binding / nuclear estrogen receptor binding / transcription coregulator activity / P-body / regulation of translation / positive regulation of cold-induced thermogenesis / molecular adaptor activity / negative regulation of translation / protein domain specific binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / RNA binding / extracellular space / nucleoplasm / membrane / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Raisch, T. / Jonas, S. / Boland, A. / Chen, Y. / Izaurralde, E. / Weichenrieder, O. | ||||||
![]() | ![]() Title: Structure and Assembly of the not Module of the Human Ccr4-not Complex Authors: Boland, A. / Chen, Y. / Raisch, T. / Jonas, S. / Kuzuoglu-Ozturk, D. / Wohlbold, L. / Weichenrieder, O. / Izaurralde, E. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. THE SHEET STRUCTURES OF CHAIN B AND C ARE BIFURCATED. ... SHEET DETERMINATION METHOD: AUTHOR PROVIDED. THE SHEET STRUCTURES OF CHAIN B AND C ARE BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED EACH FOR CHAINS B AND C. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 190.2 KB | Display | ![]() |
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PDB format | ![]() | 144.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 445.9 KB | Display | ![]() |
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Full document | ![]() | 449.5 KB | Display | |
Data in XML | ![]() | 28.6 KB | Display | |
Data in CIF | ![]() | 38.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4c0eSC ![]() 4c0fSC ![]() 4c0gSC 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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Unit cell |
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Components
#1: Protein | Mass: 92672.805 Da / Num. of mol.: 1 Fragment: NOT1 SUPERFAMILY HOMOLOGY DOMAIN, RESIDUES 1565-2371 Source method: isolated from a genetically manipulated source Details: SAMPLE WAS PROTEOLYSED PRIOR TO CRYSTALLIZATION. MOST OF THE MISSING RESIDUES (REMARK 465) ARE PROBABLY NOT IN THE CRYSTAL Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 23313.465 Da / Num. of mol.: 1 Fragment: NOT ANCHOR REGION AND NOT-BOX DOMAIN, RESIDUES 344-540 Source method: isolated from a genetically manipulated source Details: SAMPLE WAS PROTEOLYSED PRIOR TO CRYSTALLIZATION. MOST OF THE MISSING RESIDUES (REMARK 465) ARE PROBABLY NOT IN THE CRYSTAL Source: (gene. exp.) ![]() ![]() ![]() |
#3: Protein | Mass: 20224.588 Da / Num. of mol.: 1 Fragment: NOT ANCHOR REGION AND NOT-BOX DOMAIN, RESIDUES 607-753 Source method: isolated from a genetically manipulated source Details: SAMPLE WAS PROTEOLYSED PRIOR TO CRYSTALLIZATION. MOST OF THE MISSING RESIDUES (REMARK 465) ARE PROBABLY NOT IN THE CRYSTAL Source: (gene. exp.) ![]() ![]() ![]() |
Sequence details | CHAIN A, THE FIVE N-TERMINAL RESIDUES REMAIN FROM THE EXPRESSION TAG. MISSING N- AND C-TERMINI DUE ...CHAIN A, THE FIVE N-TERMINAL RESIDUES REMAIN FROM THE EXPRESSION |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3 Å3/Da / Density % sol: 59.5 % / Description: NONE |
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Crystal grow | pH: 6.5 / Details: 0.1M MES PH=6.5, 12% PEG20000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 20, 2012 / Details: DYNAMICALLY BENDABLE MIRROR |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99999 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→48.5 Å / Num. obs: 20282 / % possible obs: 98.9 % / Observed criterion σ(I): -3 / Redundancy: 3.3 % / Biso Wilson estimate: 62.8 Å2 / Rsym value: 0.12 / Net I/σ(I): 10.1 |
Reflection shell | Resolution: 3.2→3.28 Å / Redundancy: 3.4 % / Mean I/σ(I) obs: 2.2 / Rsym value: 0.56 / % possible all: 98.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRIES 4C0E, 4C0F, 4C0G Resolution: 3.2→48.48 Å / SU ML: 0.47 / σ(F): 1.99 / Phase error: 27.69 / Stereochemistry target values: ML Details: SIDE-CHAINS OF THE FOLLOWING RESIDUES WERE TRUNCATED AT CB ATOMS. CHAIN A, RESIDUES 1870, 1874, 1890, 1927, 2086, 2141, 2146, 2147, 2149, 2150, 2151, 2155, 2185, 2204, 2205, 2331, 2350, 2351. ...Details: SIDE-CHAINS OF THE FOLLOWING RESIDUES WERE TRUNCATED AT CB ATOMS. CHAIN A, RESIDUES 1870, 1874, 1890, 1927, 2086, 2141, 2146, 2147, 2149, 2150, 2151, 2155, 2185, 2204, 2205, 2331, 2350, 2351. CHAIN B, RESIDUES 368, 428, 435. CHAIN C, RESIDUES 697, 701, 713, 718, 736, 737, 745, 748.
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Solvent computation | Shrinkage radii: 0.86 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 28.472 Å2 / ksol: 0.297 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 71.5 Å2
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Refinement step | Cycle: LAST / Resolution: 3.2→48.48 Å
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Refine LS restraints |
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LS refinement shell |
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