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- PDB-2v7e: Crystal structure of coactivator-associated arginine methyltransf... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2v7e | ||||||
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Title | Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), unliganded | ||||||
![]() | HISTONE-ARGININE METHYLTRANSFERASE CARM1 | ||||||
![]() | TRANSFERASE / ARGININE METHYLTRANSFERASE / S-ADENOSYL-L-METHIONINE / TRANSCRIPTION REGULATION / HISTONE MODIFICATION / CO- ACTIVATOR / METHYLTRANSFERASE / CHROMATIN REGULATOR / NUCLEUS / TRANSCRIPTION | ||||||
Function / homology | ![]() histone H3R26 methyltransferase activity / regulation of growth plate cartilage chondrocyte proliferation / histone H3R17 methyltransferase activity / endochondral bone morphogenesis / histone H3R2 methyltransferase activity / RMTs methylate histone arginines / negative regulation of dendrite development / type I protein arginine methyltransferase / Regulation of lipid metabolism by PPARalpha / protein-arginine omega-N asymmetric methyltransferase activity ...histone H3R26 methyltransferase activity / regulation of growth plate cartilage chondrocyte proliferation / histone H3R17 methyltransferase activity / endochondral bone morphogenesis / histone H3R2 methyltransferase activity / RMTs methylate histone arginines / negative regulation of dendrite development / type I protein arginine methyltransferase / Regulation of lipid metabolism by PPARalpha / protein-arginine omega-N asymmetric methyltransferase activity / Cytoprotection by HMOX1 / protein methyltransferase activity / Estrogen-dependent gene expression / regulation of intracellular estrogen receptor signaling pathway / protein-arginine N-methyltransferase activity / replication fork reversal / histone methyltransferase activity / nuclear replication fork / positive regulation of fat cell differentiation / estrogen receptor signaling pathway / nuclear receptor-mediated steroid hormone signaling pathway / protein localization to chromatin / response to cAMP / nuclear receptor coactivator activity / lysine-acetylated histone binding / RNA polymerase II transcription regulator complex / methylation / cell population proliferation / transcription coactivator activity / transcription cis-regulatory region binding / positive regulation of cell population proliferation / regulation of DNA-templated transcription / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / protein-containing complex / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Yue, W.W. / Hassler, M. / Roe, S.M. / Thompson-Vale, V. / Pearl, L.H. | ||||||
![]() | ![]() Title: Insights Into Histone Code Syntax from Structural and Biochemical Studies of Carm1 Methyltransferase Authors: Yue, W.W. / Hassler, M. / Roe, S.M. / Thompson-Vale, V. / Pearl, L.H. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 138.6 KB | Display | ![]() |
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PDB format | ![]() | 108.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 428.4 KB | Display | ![]() |
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Full document | ![]() | 440.3 KB | Display | |
Data in XML | ![]() | 25.5 KB | Display | |
Data in CIF | ![]() | 35.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2v74C ![]() 1oriS C: citing same article ( S: Starting model for refinement |
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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 on special symmetry positions |
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Components
#1: Protein | Mass: 39104.582 Da / Num. of mol.: 2 / Fragment: CATALYTIC DOMAIN, RESIDUES 147-490 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9WVG6, Transferases; Transferring one-carbon groups; Methyltransferases #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | RESIDUES 145 AND 146 OF CHAINS A AND B ARE VECTOR-DERIVED SEQUENCE (VECTOR USED IS PFASTBAC-HTA). | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 48.99 % / Description: NONE |
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Crystal grow | pH: 7.5 Details: 1.6M DI-AMMONIUM HYDROGENPHOSPHATE, 100MM HEPES PH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: CCD / Date: Dec 11, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9776 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→30 Å / Num. obs: 19941 / % possible obs: 99.8 % / Observed criterion σ(I): 2 / Redundancy: 5.8 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 8.5 |
Reflection shell | Resolution: 2.7→2.85 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.21 / Mean I/σ(I) obs: 5.1 / % possible all: 99.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1ORI Resolution: 2.7→30.69 Å / Cor.coef. Fo:Fc: 0.914 / Cor.coef. Fo:Fc free: 0.883 / SU B: 30.831 / SU ML: 0.31 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.387 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: DISORDERED REGIONS WERE MODELED STEREOCHEMICALLY. CRYOBUFFER CONTAINS 1MM EMP. 3 PARTIALLY- DISORDERED HG ATOMS WITH LOW OCCUPANCY (< 0.5) WERE FOUND CLOSE TO CYS194 CHAIN B, CYS439 CHAIN A AND CYS421 CHAIN A.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 40.81 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→30.69 Å
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