Current Protein Identity:P06492 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
16VP CONSERVED CORE OF THE HERPES SIMPLEX VIRUS TRANSCRIPTIONAL REGULATORY PROTEIN VP16 Deposited 1999-02-11 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 47–412(366 aa) Fragment:CONSERVED CORE
Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4;pH 4.0
Resolution 2.10 Å R-free 0.260
2PHE Model for VP16 binding to PC4 Deposited 2007-04-11 Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count
Chain C 465–490(26 aa) Fragment:part of activation domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.6;298 K;Ionic strength (raw mmCIF value) 100-450 mM;Pressure 1
NMR measurement conditions pH 5.6;305 K;Ionic strength (raw mmCIF value) 100-450 mM;Pressure 1
NMR sample composition 0.2 mM VP16ad U-15N or U15N,13C, 0-0.5 mM PC4 or PC4ctd, 50 or 400 mM KCl, 50 mM phosphate buffer pH 5.6, 2 M D6-Glycine, H2O | H2O
NMR sample composition 0.2 mM PC4 or PC4ctd U-15N, 0-0.5 mM VP16ad, 50 or 400 mM KCl, 50 mM phosphate buffer pH 5.6, 2 M D6-Glycine, H2O | H2O
Resolution not provided
2PHG Model for VP16 binding to TFIIB Deposited 2007-04-11 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 465–490(26 aa) Fragment:part of activation domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.6;298 K;Ionic strength (raw mmCIF value) 100 mM;Pressure 1
NMR sample composition 0.2 mM VP16ad U-15N, 0-0.2 mM TFIIBc, 50 mM KCl, 50 mM phosphate buffer pH 5.6, 95% H2O, 5% D2O | 95% H2O/5% D2O
Resolution not provided