- PDB-4ljx: Crystal structure of an AT-rich interactive domain-containing pro... -
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Basic information
Entry
Database: PDB / ID: 4ljx
Title
Crystal structure of an AT-rich interactive domain-containing protein 3A (ARID3A) from Homo sapiens at 2.21 A resolution
Components
AT-rich interactive domain-containing protein 3A
Keywords
TRANSCRIPTION / ARID/BRIGHT DNA binding domain / PF01388 family / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-BIOLOGY / Partnership for Stem Cell Biology / STEMCELL
Function / homology
Function and homology information
TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / transcription coregulator activity / membrane raft / chromatin binding / regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / identical protein binding / nucleus / cytosol Similarity search - Function
AT-richinteractivedomain-containingprotein3A / ARID domain-containing protein 3A / B-cell regulator of IgH transcription / Bright / Dead ringer- ...ARID domain-containing protein 3A / B-cell regulator of IgH transcription / Bright / Dead ringer-like protein 1 / E2F-binding protein 1
Mass: 16258.925 Da / Num. of mol.: 2 / Fragment: ARID domain residues 216-351 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ARID3A, BC060828, DRIL1, DRIL3, DRX, E2FBP1 / Plasmid: SpeedET / Production host: Escherichia Coli (E. coli) / Strain (production host): PB1 / References: UniProt: Q99856
Mass: 18.015 Da / Num. of mol.: 55 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THE CONSTRUCT (RESIDUES 216-351) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 216-351) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 1.95 Å3/Da / Density % sol: 36.77 %
Crystal grow
Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5 Details: 20.00% PEG-6000, 0.1M Citrate pH 5.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution: 2.21→42.467 Å / Cor.coef. Fo:Fc: 0.9373 / Cor.coef. Fo:Fc free: 0.9349 / Occupancy max: 1 / Occupancy min: 0.75 / Cross valid method: THROUGHOUT / σ(F): 0 Details: 1. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED ...Details: 1. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3.NCS RESTRAINTS WERE IMPOSED BY AUTOBUSTER'S LSSR PROCEDURE (-AUTONCS).
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