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9z78

Cryo-EM structure of Enterotoxigenic Escherichia coli autotransporter A (EatA) complexed with the fragment antigen binding domain of monoclonal antibody 15

Method: ELECTRON MICROSCOPY Dmax: 140.6 Å Quality: GOOD
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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 15 × 1 Light chain of the fragment antigen binding domain of monoclonal antibody 15 × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 2.64 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.

Other PDB Difference from Current Entry 9Z78 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9Z76 Cryo-EM structure of Enterotoxigenic Escherichia coli autotransporter A (EatA) complexed with the fragment antigen binding domain of monoclonal antibody 25 Deposited 2025-11-16 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 57–1087（1031 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 3.32 Å
9Z77 Cryo-EM structure of Enterotoxigenic Escherichia coli autotransporter A (EatA) complexed with the fragment antigen binding domain of monoclonal antibody G12 Deposited 2025-11-16 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 57–1087（1031 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 3.70 Å
9Z79 Cryo-EM structure of Enterotoxigenic Escherichia coli autotransporter A (EatA) complexed with the fragment antigen binding domain of monoclonal antibody 40 Deposited 2025-11-16 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 57–1087（1031 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.66 Å

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 9z78

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9z78
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9z78
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 15
Keywords keywordsPROTEASE, BETA-HELIX, SECRETED, MONOCLONAL ANTIBODY, HYDROLASE, HYDROLASE-IMMUNE SYSTEM complex; HYDROLASE/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier41.47 Å
Radius of gyration Rg (electron density) rg_electron41.73 Å
Forward intensity I(0) i0279853000.00
Molecular weight molecular_weight133410.0 kDa
Excluded volume excluded_volume165660 ų
Envelope volume envelope_volume216260 ų
Hydration-shell volume shell_volume46189 ų
Envelope diameter envelope_diameter143.3 Å
Shell Rg shell_rg42.98 Å
Envelope Rg envelope_rg42.27 Å
Shape Rg shape_rg41.70 Å
Total Rg total_rg41.89 Å
Total atoms total_atoms9402
Residues n_residues1239
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax140.6 Å
Rg (real space) rg_real41.62 Å
Rg uncertainty (real space) rg_real_error1.51 Å
I(0) (real space) i0_real2.7990e+08
I(0) uncertainty (real space) i0_real_error5.5190e+06
Rg (reciprocal space) rg_reciprocal41.47 Å
I(0) (reciprocal space) i0_reciprocal279800000.0000
Solution quality estimate total_estimate0.8094
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.7 Å
Skewness Skewness skewness0.351
Kurtosis Kurtosis kurtosis-0.595
Angular range angular_range— – 0.1900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23670000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.916; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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8. Citations (1)

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9. Files and Curves (10)