+Open data
-Basic information
Entry | Database: PDB / ID: 2lcc | ||||||
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Title | Solution structure of RBBP1 chromobarrel domain | ||||||
Components | AT-rich interactive domain-containing protein 4A | ||||||
Keywords | TRANSCRIPTION / chromobarrel domain / RBBP1 | ||||||
Function / homology | Function and homology information establishment of Sertoli cell barrier / genomic imprinting / negative regulation of stem cell population maintenance / : / positive regulation of stem cell population maintenance / erythrocyte development / transcription repressor complex / negative regulation of cell migration / HDACs deacetylate histones / negative regulation of transforming growth factor beta receptor signaling pathway ...establishment of Sertoli cell barrier / genomic imprinting / negative regulation of stem cell population maintenance / : / positive regulation of stem cell population maintenance / erythrocyte development / transcription repressor complex / negative regulation of cell migration / HDACs deacetylate histones / negative regulation of transforming growth factor beta receptor signaling pathway / spermatogenesis / Potential therapeutics for SARS / transcription by RNA polymerase II / transcription cis-regulatory region binding / negative regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Gong, W. / Feng, Y. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2012 Title: Structural insight into recognition of methylated histone tails by retinoblastoma-binding protein 1. Authors: Gong, W. / Zhou, T. / Mo, J. / Perrett, S. / Wang, J. / Feng, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lcc.cif.gz | 489.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lcc.ent.gz | 412.4 KB | Display | PDB format |
PDBx/mmJSON format | 2lcc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lc/2lcc ftp://data.pdbj.org/pub/pdb/validation_reports/lc/2lcc | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 9082.257 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 568-635 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ARID4A, RBBP1, RBP1 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta (DE3) / References: UniProt: P29374 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.4 / pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |