7s5s

CTX-M-15 WT in complex with BLIP WT

Method: X-RAY DIFFRACTION Dmax: 72.6 Å Quality: GOOD

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

Beta-lactamase

Escherichia coli

UniProt C7S9T0

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 50–311 Not recorded Beta-lactamase inhibitory protein × 1 (P35804) 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

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.

4 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C7S9T0_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–262; UniProt 50–311

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 (C7S9T0) 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

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 1–165; 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 7s5s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7s5s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7s5s
Deposition date deposition_date2021-09-11
Structure title titleCTX-M-15 WT in complex with BLIP WT
Keywords keywordsBeta-lactamase, antibiotic resistance, Beta-lactamase inhibitory protein, protein complex, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.59
Radius of gyration Rg (electron density) rg_electron21.75
Forward intensity I(0) i036364100.00
Molecular weight molecular_weight45448.0 kDa
Excluded volume excluded_volume56495 ų
Envelope volume envelope_volume63902 ų
Hydration-shell volume shell_volume24427 ų
Envelope diameter envelope_diameter73.4
Shell Rg shell_rg28.85
Envelope Rg envelope_rg22.03
Shape Rg shape_rg21.72
Total Rg total_rg22.65
Total atoms total_atoms3194
Residues n_residues427
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 dmax72.6
Rg (real space) rg_real22.53
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real3.6360e+07
I(0) uncertainty (real space) i0_real_error4.5530e+05
Rg (reciprocal space) rg_reciprocal22.55
I(0) (reciprocal space) i0_reciprocal36360000.0000
Solution quality estimate total_estimate0.8940
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.4
Skewness Skewness skewness0.295
Kurtosis Kurtosis kurtosis-0.353
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9623000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.888; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7s5sA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology710 — Beta-lactamase
Homologous superfamily homologous superfamily10 — DD-peptidase/beta-lactamase superfamily

8. Citations (1)

9. Files and Curves (10)