SAXSdb — 3c7v

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Beta-lactamase

Escherichia coli

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 24–286	Mutation：Y51A	Beta-lactamase inhibitory protein × 1 （P35804）	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
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 24–286	Mutation：Y51A	Beta-lactamase inhibitory protein × 1 （P35804）	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

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 3C7V	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3C7U Structural Insight into the Kinetics and Cp of interactions between TEM-1-Lactamase and BLIP Deposited 2008-02-08	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	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	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	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
3DTM Increased folding stability of TEM-1 beta-lactamase by in-vitro selection Deposited 2008-07-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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

4 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q79DR3_ECOLX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–263； UniProt 24–286 Author chain C； PDBConstruct 1–263； UniProt 24–286

Beta-lactamase inhibitory protein

Streptomyces clavuligerus

UniProt P35804

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 37–201	Not recorded	Beta-lactamase × 1 （Q79DR3）	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
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 37–201	Not recorded	Beta-lactamase × 1 （Q79DR3）	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

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 3C7V	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1JTG CRYSTAL STRUCTURE OF TEM-1 BETA-LACTAMASE / BETA-LACTAMASE INHIBITOR PROTEIN COMPLEX Deposited 2001-08-20	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 37–201（165 aa）	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.8；pH 8.8	Resolution 1.73 Å R-free 0.205
1JTG CRYSTAL STRUCTURE OF TEM-1 BETA-LACTAMASE / BETA-LACTAMASE INHIBITOR PROTEIN COMPLEX Deposited 2001-08-20	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 37–201（165 aa）	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.8；pH 8.8	Resolution 1.73 Å R-free 0.205
1S0W 1b Lactamse/ b Lactamase Inhibitor Deposited 2004-01-05	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 37–201（165 aa）	Mutation：F1142A	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 7.5；293 K；PEG 8000, Dioxane, pH 7.5, Microbatch, temperature 293K	Resolution 2.30 Å
1S0W 1b Lactamse/ b Lactamase Inhibitor Deposited 2004-01-05	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 37–201（165 aa）	Mutation：F1142A	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 7.5；293 K；PEG 8000, Dioxane, pH 7.5, Microbatch, temperature 293K	Resolution 2.30 Å
1XXM The modular architecture of protein-protein binding site Deposited 2004-11-07	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 37–201（165 aa）	Mutation：K74A; F142A; Y143A	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 5；298 K；LiCl; sodium Acetate; PEG 6000, pH 5., Microbatch, temperature 298K	Resolution 1.90 Å R-free 0.247
1XXM The modular architecture of protein-protein binding site Deposited 2004-11-07	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 37–201（165 aa）	Mutation：K74A; F142A; Y143A	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 5；298 K；LiCl; sodium Acetate; PEG 6000, pH 5., Microbatch, temperature 298K	Resolution 1.90 Å R-free 0.247
2B5R 1B Lactamase / B Lactamase Inhibitor Deposited 2005-09-29	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 37–201（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；298 K；PEG 3350, NH4 Acetate, pH 8.5, Microbatch, temperature 298K	Resolution 1.65 Å R-free 0.222
2B5R 1B Lactamase / B Lactamase Inhibitor Deposited 2005-09-29	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 37–201（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；298 K；PEG 3350, NH4 Acetate, pH 8.5, Microbatch, temperature 298K	Resolution 1.65 Å R-free 0.222
2G2U Crystal Structure of the SHV-1 Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) complex Deposited 2006-02-16	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 37–201（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；293 K；30% Ammonium SO4,25mM cacodylate, 10mM BisTris, 25mM NaCl , pH 6.5, EVAPORATION, temperature 293K	Resolution 1.60 Å R-free 0.186
2G2W Crystal Structure of the SHV D104K Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) complex Deposited 2006-02-16	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 37–201（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；293 K；4% PEG 8000, 25mM cacodylate, 10 mM BisTris, 25mM NaCl, pH 6.5, EVAPORATION, temperature 293K	Resolution 1.80 Å R-free 0.222
3C4O Crystal Structure of the SHV-1 Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) E73M/S130K/S146M complex Deposited 2008-01-30	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 37–201（165 aa）	Mutation：E109M,S166K,S182M	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.4；292 K；37.5% Ammonium Sulfate, 100mM Tris HCl, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 1.70 Å R-free 0.196
3C4P Crystal Structure of the SHV-1 Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) E73M complex Deposited 2008-01-30	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 37–201（165 aa）	Mutation：E109M	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.4；292 K；37.5% Ammonium Sulfate, 100mM Tris HCl, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 1.75 Å R-free 0.207
3C7U Structural Insight into the Kinetics and Cp of interactions between TEM-1-Lactamase and BLIP Deposited 2008-02-08	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 37–201（165 aa）	Not recorded	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	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 37–201（165 aa）	Not recorded	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
3E2K Crystal Structure of the KPC-2 Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) Deposited 2008-08-05	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 37–201（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；290 K；20% PEG 8000, 4% ethylene glycol, 100mM citrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.10 Å R-free 0.234
3E2K Crystal Structure of the KPC-2 Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) Deposited 2008-08-05	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 37–201（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；290 K；20% PEG 8000, 4% ethylene glycol, 100mM citrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.10 Å R-free 0.234
3E2L Crystal Structure of the KPC-2 Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) Deposited 2008-08-05	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 37–201（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；290 K；20% PEG 8000, 6% ethylene glycol, 100mM citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 1.87 Å R-free 0.213
3E2L Crystal Structure of the KPC-2 Beta-lactamase/Beta-lactamase inhibitor protein (BLIP) Deposited 2008-08-05	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 37–201（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；290 K；20% PEG 8000, 6% ethylene glycol, 100mM citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 1.87 Å R-free 0.213
3GMU Crystal Structure of Beta-Lactamse Inhibitory Protein (BLIP) in Apo Form Deposited 2009-03-15	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 37–201（165 aa）	Not recorded	NH4 AMMONIUM ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；298 K；10 mg/ml protein, 20% saturated ammonium sulfate, 50 mM sodium citrate, pH 5.5, vapor diffusion, temperature 298K	Resolution 1.98 Å R-free 0.229
3N4I Crystal structure of the SHV-1 D104E beta-lactamase/beta-lactamase inhibitor protein (BLIP) complex Deposited 2010-05-21	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 37–201（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；40% ammonium sulfate, 100mM Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.56 Å R-free 0.179
7S5S CTX-M-15 WT in complex with BLIP WT Deposited 2021-09-11	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 37–201（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% w/v PEG3350, 0.2 M NaF, 0.1 M Bis-Tris-propane pH 6.5	Resolution 1.40 Å R-free 0.166
9Q0A CTX-M-14 WT in complex with BLIP E73W Deposited 2025-08-12	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 37–201（165 aa）	Mutation：E73W	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.2 M calcium chloride, 0.1 M sodium acetate pH 5, 20% (w/v) PEG 6000	Resolution 1.65 Å R-free 0.211
9Q0B CTX-M-15 WT in complex with BLIP E73W Deposited 2025-08-12	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 38–201（164 aa）	Mutation：E73W	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.1 M MES pH 6.5, 25% (w/v) PEG 4000	Resolution 1.58 Å R-free 0.182
9Q0C TEM-1 WT in complex with BLIP E73W Deposited 2025-08-12	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 37–201（165 aa）	Mutation：E73W	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.1 M magnesium chloride, 0.1 M sodium acetate pH 4.6, 25% (w/v) PEG 400	Resolution 1.78 Å R-free 0.215
9Q0C TEM-1 WT in complex with BLIP E73W Deposited 2025-08-12	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 37–201（165 aa）	Mutation：E73W	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.1 M magnesium chloride, 0.1 M sodium acetate pH 4.6, 25% (w/v) PEG 400	Resolution 1.78 Å R-free 0.215

17 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BLIP_STRCL
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–165； UniProt 37–201 Author chain D； PDBConstruct 1–165； UniProt 37–201

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3c7v
Deposition date deposition_date	2008-02-08
Structure title title	Structural Insight into the Kinetics and Delta-Cp of interactions between TEM-1 Beta-Lactamase and BLIP
Keywords keywords	enzyme-inhibitor complex, Antibiotic resistance, Hydrolase, Plasmid, Secreted, HYDROLASE-HYDROLASE INHIBITOR COMPLEX; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	34.92 Å
Radius of gyration Rg (electron density) rg_electron	34.68 Å
Forward intensity I(0) i0	138769000.00
Molecular weight molecular_weight	92781.0 kDa
Excluded volume excluded_volume	115400 Å³
Envelope volume envelope_volume	145960 Å³
Hydration-shell volume shell_volume	35818 Å³
Envelope diameter envelope_diameter	113.1 Å
Shell Rg shell_rg	40.41 Å
Envelope Rg envelope_rg	33.87 Å
Shape Rg shape_rg	34.67 Å
Total Rg total_rg	35.12 Å
Total atoms total_atoms	6516
Residues n_residues	856
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	111.6 Å
Rg (real space) rg_real	35.00 Å
Rg uncertainty (real space) rg_real_error	0.88 Å
I(0) (real space) i0_real	1.3880e+08
I(0) uncertainty (real space) i0_real_error	1.8960e+06
Rg (reciprocal space) rg_reciprocal	34.95 Å
I(0) (reciprocal space) i0_reciprocal	138800000.0000
Solution quality estimate total_estimate	0.8780
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	29.8 Å
Skewness Skewness skewness	0.268
Kurtosis Kurtosis kurtosis	-0.816
Angular range angular_range	— – 0.2250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	23630000.0000
Real-space data points n_real_points	46
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.902; Smooth: 0.912

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Beta-lactamase
Molecular weight formula_weight	28984.1 kDa
EC 编号 ec_number	3.5.2.6
Mutation mutation	Y51A
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	6689

HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVLLCGAVLSRIDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTMPVAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASLIKHW

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Beta-lactamase inhibitory protein
Molecular weight formula_weight	17464.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

AGVMTGAKFTQIQFGMTRQQVLDIAGAENCETGGSFGDSIHCRGHAAGDYAAYATFGFTSAAADAKVDSKSQEKLLAPSAPTLTLAKFNQVTVGMTRAQVLATVGQGSCTTWSEYYPAYPSTAGVTLSLSCFDVDGYSSTGFYRGSAHLWFTDGVLQGKRQWDLV

来源 Source

来源生物 organism	Streptomyces clavuligerus
NCBI Class编号 ncbi_taxonomy_id	1901
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	173

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7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3c7va_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.3 — beta-lactamase/transpeptidase-like
Superfamily Superfamily superfamily	e.3.1 — beta-lactamase/transpeptidase-like
Family Family family	e.3.1.1 — beta-Lactamase/D-ala carboxypeptidase

Domain ID domain_id	d3c7vb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.98 — BLIP-like
Superfamily Superfamily superfamily	d.98.1 — beta-lactamase-inhibitor protein, BLIP
Family Family family	d.98.1.1 — beta-lactamase-inhibitor protein, BLIP

Domain ID domain_id	d3c7vc_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.3 — beta-lactamase/transpeptidase-like
Superfamily Superfamily superfamily	e.3.1 — beta-lactamase/transpeptidase-like
Family Family family	e.3.1.1 — beta-Lactamase/D-ala carboxypeptidase

Domain ID domain_id	d3c7vd_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.98 — BLIP-like
Superfamily Superfamily superfamily	d.98.1 — beta-lactamase-inhibitor protein, BLIP
Family Family family	d.98.1.1 — beta-lactamase-inhibitor protein, BLIP

CATH v4.4 (6 domains)

Domain ID domain_id	3c7vA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	710 — Beta-lactamase
Homologous superfamily homologous superfamily	10 — DD-peptidase/beta-lactamase superfamily

Domain ID domain_id	3c7vB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1450 — Beta-lactamase Inhibitory Protein; Chain:B, domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	3c7vB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1450 — Beta-lactamase Inhibitory Protein; Chain:B, domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	3c7vC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	710 — Beta-lactamase
Homologous superfamily homologous superfamily	10 — DD-peptidase/beta-lactamase superfamily

Domain ID domain_id	3c7vD01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1450 — Beta-lactamase Inhibitory Protein; Chain:B, domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	3c7vD02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1450 — Beta-lactamase Inhibitory Protein; Chain:B, domain 1
Homologous superfamily homologous superfamily	10 —

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8. Citations (1)

▶

Unit-cell length a length_a	48.671 Å
Unit-cell length b length_b	129.044 Å
Unit-cell length c length_c	78.898 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.20 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.070 Å
Low-resolution limit resolution_low	35.090 Å
R factor r_factor	0.2156
R_work r_work	0.2144
R_free r_free	0.2385

fit	/app/data/saxs_computation/c7/3c7v/3c7v.fit
pddf	/app/data/pr_computation/c7/3c7v/3c7v.pr.out
profile	/app/data/saxs_computation/c7/3c7v/3c7v.dat

Structural Insight into the Kinetics and Delta-Cp of interactions between TEM-1 Beta-Lactamase and BLIP

1. Protein Identity and Related Structures Protein Identity & Related Structures

Beta-lactamase

State in the Current Structure

Other States of the Same Protein in the Database

Beta-lactamase inhibitory protein

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

CATH v4.4 (6 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)