9q0c

TEM-1 WT in complex with BLIP E73W

Method: X-RAY DIFFRACTION Dmax: 97.1 Å Quality: EXCELLENT

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

Beta-lactamase TEM

Escherichia coli

UniProt P62593

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 Not recorded Beta-lactamase inhibitory protein × 1 (P35804) 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
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 24–286 Not recorded Beta-lactamase inhibitory protein × 1 (P35804) 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

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.

72 other PDB entries and 154 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BLAT_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 Mutation:E73W Beta-lactamase TEM × 1 (P62593) 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
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 37–201 Mutation:E73W Beta-lactamase TEM × 1 (P62593) 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

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.

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.

SAXS scattering curve SAXS Profile

SAXS profile for 9q0c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9q0c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9q0c
Deposition date deposition_date2025-08-12
Structure title titleTEM-1 WT in complex with BLIP E73W
Keywords keywordsbeta-lactamase, inhibitory, protein, BLIP, TEM, PROTEIN BINDING, HYDROLASE-PROTEIN BINDING complex; HYDROLASE/PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.56
Radius of gyration Rg (electron density) rg_electron29.99
Forward intensity I(0) i0141193000.00
Molecular weight molecular_weight92926.0 kDa
Excluded volume excluded_volume115610 ų
Envelope volume envelope_volume137020 ų
Hydration-shell volume shell_volume38028 ų
Envelope diameter envelope_diameter101.5
Shell Rg shell_rg37.25
Envelope Rg envelope_rg29.84
Shape Rg shape_rg29.98
Total Rg total_rg30.61
Total atoms total_atoms6529
Residues n_residues855
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax97.1
Rg (real space) rg_real30.52
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.4120e+08
I(0) uncertainty (real space) i0_real_error2.0350e+06
Rg (reciprocal space) rg_reciprocal30.54
I(0) (reciprocal space) i0_reciprocal141200000.0000
Solution quality estimate total_estimate0.9013
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.6
Skewness Skewness skewness0.281
Kurtosis Kurtosis kurtosis-0.511
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha39000000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.921

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)