9q0b

CTX-M-15 WT in complex with BLIP E73W

Method: X-RAY DIFFRACTION Dmax: 72.3 Å Quality: GOOD

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

Beta-lactamase CTX-M-15

Escherichia coli

UniProt A0A5R8T042

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 31–291 Not recorded Beta-lactamase inhibitory protein × 1 (P35804) 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

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name BLC15_ECO25
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–261; UniProt 31–291

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 38–201 Mutation:E73W Beta-lactamase CTX-M-15 × 1 (A0A5R8T042) 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

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 26 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 1–164; UniProt 38–201

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 9q0b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9q0b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9q0b
Deposition date deposition_date2025-08-12
Structure title titleCTX-M-15 WT in complex with BLIP E73W
Keywords keywordsbeta-lactamase, BLIP, beta-lactamase inhibitory protein, 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_guinier22.61
Radius of gyration Rg (electron density) rg_electron21.75
Forward intensity I(0) i036169000.00
Molecular weight molecular_weight45392.0 kDa
Excluded volume excluded_volume56451 ų
Envelope volume envelope_volume64325 ų
Hydration-shell volume shell_volume24574 ų
Envelope diameter envelope_diameter73.4
Shell Rg shell_rg28.77
Envelope Rg envelope_rg22.00
Shape Rg shape_rg21.73
Total Rg total_rg22.65
Total atoms total_atoms3191
Residues n_residues425
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 dmax72.3
Rg (real space) rg_real22.55
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real3.6170e+07
I(0) uncertainty (real space) i0_real_error4.7510e+05
Rg (reciprocal space) rg_reciprocal22.57
I(0) (reciprocal space) i0_reciprocal36170000.0000
Solution quality estimate total_estimate0.8958
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4
Skewness Skewness skewness0.284
Kurtosis Kurtosis kurtosis-0.366
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9750000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.959

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)