9me4

Antibody fragments from mAb475 and mAb824 bound to the adhesin protein FimH

Method: ELECTRON MICROSCOPY Dmax: 161.1 Å Quality: REASONABLE

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

Type 1 fimbrin D-mannose specific adhesin

Escherichia coli

UniProt P08191

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 其他Polymer 1 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–300 Not recorded Protein FimG × 1 (P08190) mAb475 Heavy Chain Fragment × 1 mAb824 Heavy Chain Fragment × 1 mAb475 Light Chain Fragment × 1 mAb824 Light Chain Fragment × 1 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

57 other PDB entries and 138 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMH_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–300; UniProt 1–300

Protein FimG

Escherichia coli K-12

UniProt P08190

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 其他Polymer 1 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 1–167 Not recorded Type 1 fimbrin D-mannose specific adhesin × 1 (P08191) mAb475 Heavy Chain Fragment × 1 mAb824 Heavy Chain Fragment × 1 mAb475 Light Chain Fragment × 1 mAb824 Light Chain Fragment × 1 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

15 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMG_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–167; UniProt 1–167

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 9me4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9me4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9me4
Deposition date deposition_date2024-12-06
Structure title titleAntibody fragments from mAb475 and mAb824 bound to the adhesin protein FimH
Keywords keywordsFimbrial tip, Lectin domain, Antibody fragments, Antibody-target complex, CELL ADHESION, CELL ADHESION-IMMUNE SYSTEM complex; CELL ADHESION/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.34
Radius of gyration Rg (electron density) rg_electron44.59
Forward intensity I(0) i0233262000.00
Molecular weight molecular_weight121970.0 kDa
Excluded volume excluded_volume151430 ų
Envelope volume envelope_volume221340 ų
Hydration-shell volume shell_volume44735 ų
Envelope diameter envelope_diameter168.0
Shell Rg shell_rg44.42
Envelope Rg envelope_rg44.44
Shape Rg shape_rg44.54
Total Rg total_rg44.73
Total atoms total_atoms8583
Residues n_residues1124
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 dmax161.1
Rg (real space) rg_real44.67
Rg uncertainty (real space) rg_real_error2.41
I(0) (real space) i0_real2.3330e+08
I(0) uncertainty (real space) i0_real_error4.9380e+06
Rg (reciprocal space) rg_reciprocal44.34
I(0) (reciprocal space) i0_reciprocal233200000.0000
Solution quality estimate total_estimate0.6112
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.3
Skewness Skewness skewness0.452
Kurtosis Kurtosis kurtosis-0.231
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14830000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.713; Stabil: 1.000; Sysdev: 0.145; Positv: 1.000; Valcen: 0.705; Smooth: 0.661

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)