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Open data
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Basic information
Entry | Database: PDB / ID: 2b2y | ||||||
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Title | Tandem chromodomains of human CHD1 | ||||||
![]() | (Chromodomain-helicase-DNA-binding protein 1) x 2 | ||||||
![]() | PEPTIDE BINDING PROTEIN / CHD / Chromodomain / three stranded antiparallel Beta sheet / alpha helix linker | ||||||
Function / homology | ![]() nucleosome organization / ATP-dependent chromatin remodeler activity / positive regulation by host of viral transcription / nuclear chromosome / forked DNA-dependent helicase activity / single-stranded 3'-5' DNA helicase activity / four-way junction helicase activity / double-stranded DNA helicase activity / methylated histone binding / histone binding ...nucleosome organization / ATP-dependent chromatin remodeler activity / positive regulation by host of viral transcription / nuclear chromosome / forked DNA-dependent helicase activity / single-stranded 3'-5' DNA helicase activity / four-way junction helicase activity / double-stranded DNA helicase activity / methylated histone binding / histone binding / chromatin extrusion motor activity / ATP-dependent H2AZ histone chaperone activity / ATP-dependent H3-H4 histone complex chaperone activity / DNA helicase / cohesin loader activity / DNA clamp loader activity / Estrogen-dependent gene expression / chromatin remodeling / chromatin binding / chromatin / ATP hydrolysis activity / DNA binding / nucleoplasm / ATP binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Flanagan IV, J.F. / Mi, L.-Z. / Chruszcz, M. / Cymborowski, M. / Clines, K.L. / Kim, Y. / Minor, W. / Rastinejad, F. / Khorasanizadeh, S. | ||||||
![]() | ![]() Title: Double chromodomains cooperate to recognize the methylated histone H3 tail. Authors: Flanagan, J.F. / Mi, L.Z. / Chruszcz, M. / Cymborowski, M. / Clines, K.L. / Kim, Y. / Minor, W. / Rastinejad, F. / Khorasanizadeh, S. | ||||||
History |
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Remark 300 | BIOMOLECULE THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 3 CHAIN(S). ...BIOMOLECULE THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 3 CHAIN(S). ACCORDING TO AUTHORS, THE BIOLOGICAL UNIT IS UNKNOWN. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 104.7 KB | Display | ![]() |
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PDB format | ![]() | 79.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 451.7 KB | Display | ![]() |
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Full document | ![]() | 465.7 KB | Display | |
Data in XML | ![]() | 21.3 KB | Display | |
Data in CIF | ![]() | 29.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2b2tSC ![]() 2b2uC ![]() 2b2vC ![]() 2b2wC 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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1 |
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Unit cell |
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Components
#1: Protein | Mass: 22146.762 Da / Num. of mol.: 2 / Fragment: residues 268-443 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | | Mass: 13694.292 Da / Num. of mol.: 1 / Fragment: residues 268-373 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 49 % |
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Crystal grow | Temperature: 283 K / pH: 8 Details: 4% PEG3350, 0.05M HEPES, 10mM BTP, pH 8.0, 12.5mM NaCl, 5mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 283K, pH 8.00 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Mar 15, 2004 |
Radiation | Monochromator: DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97928 Å / Relative weight: 1 |
Reflection | Resolution: 2.35→31.3 Å / Num. obs: 21913 / % possible obs: 91.1 % / Redundancy: 3.4 % / Rsym value: 0.088 / Net I/σ(I): 11.6 |
Reflection shell | Resolution: 2.35→2.43 Å / Redundancy: 2.4 % / Mean I/σ(I) obs: 3.2 / Rsym value: 0.254 / % possible all: 76.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2B2T without chain D Resolution: 2.35→15 Å / Isotropic thermal model: ISOTROPIC / σ(F): 3580 / Stereochemistry target values: Engh & Huber
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Solvent computation | Bsol: 37.66 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 46.23 Å2
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Refinement step | Cycle: LAST / Resolution: 2.35→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.35→2.43 Å / Total num. of bins used: 10
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Xplor file |
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