9z76

Cryo-EM structure of Enterotoxigenic Escherichia coli autotransporter A (EatA) complexed with the fragment antigen binding domain of monoclonal antibody 25

Method: ELECTRON MICROSCOPY Dmax: 104.1 Å Quality: REASONABLE

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

Serine protease EatA

Escherichia coli

UniProt Q84GK0

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 57–1087 Not recorded Heavy chain of the fragment antigen binding domain of monoclonal antibody 25 × 1 Light chain of the fragment antigen binding domain of monoclonal antibody 25 × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.32 Å

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EATA_ECOH1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1031; UniProt 57–1087

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 9z76

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9z76
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9z76
Deposition date deposition_date2025-11-16
Structure title titleCryo-EM structure of Enterotoxigenic Escherichia coli autotransporter A (EatA) complexed with the fragment antigen binding domain of monoclonal antibody 25
Keywords keywordsPROTEASE, BETA-HELIX, SECRETED, MONOCLONAL ANTIBODY, HYDROLASE, HYDROLASE-IMMUNE SYSTEM complex; HYDROLASE/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.95
Radius of gyration Rg (electron density) rg_electron30.52
Forward intensity I(0) i0106456000.00
Molecular weight molecular_weight79769.0 kDa
Excluded volume excluded_volume98734 ų
Envelope volume envelope_volume128790 ų
Hydration-shell volume shell_volume35576 ų
Envelope diameter envelope_diameter112.6
Shell Rg shell_rg37.04
Envelope Rg envelope_rg30.58
Shape Rg shape_rg30.52
Total Rg total_rg31.08
Total atoms total_atoms5657
Residues n_residues840
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 dmax104.1
Rg (real space) rg_real31.00
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real1.0650e+08
I(0) uncertainty (real space) i0_real_error2.0080e+06
Rg (reciprocal space) rg_reciprocal30.98
I(0) (reciprocal space) i0_reciprocal106500000.0000
Solution quality estimate total_estimate0.6695
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.7
Skewness Skewness skewness0.394
Kurtosis Kurtosis kurtosis-0.259
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45050000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.856; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.937; Smooth: 0.851

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)