Current Protein Identity:P60338 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion 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
1AIP EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS Deposited 1997-04-22 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–405(405 aa)
Chain B 1–405(405 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5;60 MM CACODYLATE, PH 6.5 70 MM AMMONIUM SULFATE 8% PEG 8000
Resolution 3.00 Å R-free 0.289
1AIP EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS Deposited 1997-04-22 Assembly 2 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain E 1–405(405 aa)
Chain F 1–405(405 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5;60 MM CACODYLATE, PH 6.5 70 MM AMMONIUM SULFATE 8% PEG 8000
Resolution 3.00 Å R-free 0.289
1EXM CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS ELONGATION FACTOR TU (EF-TU) IN COMPLEX WITH THE GTP ANALOGUE GPPNHP. Deposited 2000-05-03 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 2–406(405 aa) Fragment:INTACT WILD-TYPE EF-TU
Not recorded MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;20mM Sodium cacodylate, 5mM Magnesium sulfate, 38-44% Ammonium sulfate, 7-10 mg/mL EF-Tu, molar ratio EF-Tu:GppNHp = 1:5, pH 7.0, VAPOR DIFFUSION, HANGING DROP
Resolution 1.70 Å R-free 0.243
4H9G Probing EF-Tu with a very small brominated fragment library identifies the CCA pocket Deposited 2012-09-24 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 2–406(405 aa)
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 NH4 AMMONIUM ION × 1 SO4 SULFATE ION × 8 14J 5-bromofuran-2-carboxylic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.6;292 K;1.8M ammonium sulfate, 15% sucrose, 0.1M tris, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 1.93 Å R-free 0.184
4LBV Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 3–406(404 aa)
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 NH4 AMMONIUM ION × 1 CL CHLORIDE ION × 1 SO4 SULFATE ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.6;292 K;1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.03 Å R-free 0.193
4LBV Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 3–406(404 aa)
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 NH4 AMMONIUM ION × 2 CL CHLORIDE ION × 2 SO4 SULFATE ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.6;292 K;1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.03 Å R-free 0.193
4LBW Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 3–406(404 aa)
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 NH4 AMMONIUM ION × 1 SO4 SULFATE ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.6;292 K;1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 1.74 Å R-free 0.194
4LBW Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 3–406(404 aa)
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 NH4 AMMONIUM ION × 2 SO4 SULFATE ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.6;292 K;1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 1.74 Å R-free 0.194
4LBY Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 3–406(404 aa)
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 NH4 AMMONIUM ION × 1 SO4 SULFATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.6;292 K;1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.69 Å R-free 0.207
4LBZ Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 3–406(404 aa)
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 NH4 AMMONIUM ION × 1 SO4 SULFATE ION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.6;292 K;1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.22 Å R-free 0.212
4LBZ Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 3–406(404 aa)
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 NH4 AMMONIUM ION × 2 SO4 SULFATE ION × 14 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.6;292 K;1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.22 Å R-free 0.212
4LC0 Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 3–406(404 aa)
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 NH4 AMMONIUM ION × 1 SO4 SULFATE ION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.6;292 K;1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.22 Å R-free 0.201
4LC0 Identifying ligand binding hot spots in proteins using brominated fragments Deposited 2013-06-21 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 3–406(404 aa)
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 NH4 AMMONIUM ION × 2 SO4 SULFATE ION × 14 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.6;292 K;1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 2.22 Å R-free 0.201