Current Protein Identity:Q79DR3 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
3C7U Structural Insight into the Kinetics and Cp of interactions between TEM-1-Lactamase and BLIP Deposited 2008-02-08 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 24–286(263 aa)
Mutation:W150A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 4.5;298 K;15% PEG 8000, 0.1M Phosphate-Citrate, 0.1M NaCl, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.20 Å R-free 0.232
3C7U Structural Insight into the Kinetics and Cp of interactions between TEM-1-Lactamase and BLIP Deposited 2008-02-08 Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain C 24–286(263 aa)
Mutation:W150A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 4.5;298 K;15% PEG 8000, 0.1M Phosphate-Citrate, 0.1M NaCl, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.20 Å R-free 0.232
3C7V Structural Insight into the Kinetics and Delta-Cp of interactions between TEM-1 Beta-Lactamase and BLIP Deposited 2008-02-08 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 24–286(263 aa)
Mutation:Y51A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 4.2;298 K;12% PEG 8000, 0.1M Phosphate-Citrate, 0.1M NaCl, pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.07 Å R-free 0.238
3C7V Structural Insight into the Kinetics and Delta-Cp of interactions between TEM-1 Beta-Lactamase and BLIP Deposited 2008-02-08 Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain C 24–286(263 aa)
Mutation:Y51A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 4.2;298 K;12% PEG 8000, 0.1M Phosphate-Citrate, 0.1M NaCl, pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.07 Å R-free 0.238
3DTM Increased folding stability of TEM-1 beta-lactamase by in-vitro selection Deposited 2008-07-15 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 24–286(263 aa) Fragment:UNP residues 24-286
Mutation:P62S, V80I, E147G, M182T, L201P, I208M, A224V, I246V, L273R No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;288 K;1.6-1.8 M Ammonium citrate, 5% PEG 400, 0.1M Tris buffer, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 288K
Resolution 2.00 Å R-free 0.272
3TOI Tailoring Enzyme Stability and Exploiting Stability-Trait Linkage by Iterative Truncation and Optimization Deposited 2011-09-05 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 39–283(245 aa) Fragment:UNP residues 39-283
Mutation:I56V, R120G, M182T, T195S, I208M, A224V, R241H, T265M No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;0.2 M imidazole maleate, 44% PEG600, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K
Resolution 1.90 Å R-free 0.237
3TOI Tailoring Enzyme Stability and Exploiting Stability-Trait Linkage by Iterative Truncation and Optimization Deposited 2011-09-05 Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain B 39–283(245 aa) Fragment:UNP residues 39-283
Mutation:I56V, R120G, M182T, T195S, I208M, A224V, R241H, T265M No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;0.2 M imidazole maleate, 44% PEG600, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K
Resolution 1.90 Å R-free 0.237
4OQG Crystal structure of TEM-1 beta-lactamase in complex with boron-based inhibitor EC25 Deposited 2014-02-09 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 24–286(263 aa) Fragment:TEM-1
Not recorded 2UL 3-[(2R)-2-{[(2R)-2-amino-2-phenylacetyl]amino}-2-(dihydroxyboranyl)ethyl]benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.2;293 K;6% PEG 8000, 100 mM MES buffer, 200mM Ca(OAc)2 and 50 M NaF, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.40 Å R-free 0.264
4OQG Crystal structure of TEM-1 beta-lactamase in complex with boron-based inhibitor EC25 Deposited 2014-02-09 Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain B 24–286(263 aa) Fragment:TEM-1
Not recorded 2UL 3-[(2R)-2-{[(2R)-2-amino-2-phenylacetyl]amino}-2-(dihydroxyboranyl)ethyl]benzoic acid × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.2;293 K;6% PEG 8000, 100 mM MES buffer, 200mM Ca(OAc)2 and 50 M NaF, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.40 Å R-free 0.264
4OQG Crystal structure of TEM-1 beta-lactamase in complex with boron-based inhibitor EC25 Deposited 2014-02-09 Assembly 3 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain C 24–286(263 aa) Fragment:TEM-1
Not recorded 2UL 3-[(2R)-2-{[(2R)-2-amino-2-phenylacetyl]amino}-2-(dihydroxyboranyl)ethyl]benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.2;293 K;6% PEG 8000, 100 mM MES buffer, 200mM Ca(OAc)2 and 50 M NaF, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.40 Å R-free 0.264
4OQG Crystal structure of TEM-1 beta-lactamase in complex with boron-based inhibitor EC25 Deposited 2014-02-09 Assembly 4 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain D 24–286(263 aa) Fragment:TEM-1
Not recorded 2UL 3-[(2R)-2-{[(2R)-2-amino-2-phenylacetyl]amino}-2-(dihydroxyboranyl)ethyl]benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.2;293 K;6% PEG 8000, 100 mM MES buffer, 200mM Ca(OAc)2 and 50 M NaF, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.40 Å R-free 0.264
4OQG Crystal structure of TEM-1 beta-lactamase in complex with boron-based inhibitor EC25 Deposited 2014-02-09 Assembly 5 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain E 24–286(263 aa) Fragment:TEM-1
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.2;293 K;6% PEG 8000, 100 mM MES buffer, 200mM Ca(OAc)2 and 50 M NaF, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.40 Å R-free 0.264
4OQG Crystal structure of TEM-1 beta-lactamase in complex with boron-based inhibitor EC25 Deposited 2014-02-09 Assembly 6 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain F 24–286(263 aa) Fragment:TEM-1
Not recorded 2UL 3-[(2R)-2-{[(2R)-2-amino-2-phenylacetyl]amino}-2-(dihydroxyboranyl)ethyl]benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.2;293 K;6% PEG 8000, 100 mM MES buffer, 200mM Ca(OAc)2 and 50 M NaF, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.40 Å R-free 0.264