9d6f

Cryo-EM structure of E. coli FimH lectin domain bound to Fabs 440-2 and 454-3

Method: ELECTRON MICROSCOPY Dmax: 105.3 Å Quality: GOOD

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

;Type 1 fimbrin D-mannose specific adhesin FimH, Donor strand complemented with FimG peptide 'triple mutant' ;

Escherichia coli

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 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 24–37 Mutation:N7S, G15A, G16A, V27A, N70S, N228Q within FimH 440-2 Fab light chain × 1 440-2 Fab heavy chain × 1 445-3 Fab heavy chain × 1 445-3 Fab light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.24 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 5
Chains and sequence ranges Author chain D; PDBConstruct 287–300; UniProt 24–37

;Type 1 fimbrin D-mannose specific adhesin FimH, Donor strand complemented with FimG peptide 'triple mutant' ;

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 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 22–300 Mutation:N7S, G15A, G16A, V27A, N70S, N228Q within FimH 440-2 Fab light chain × 1 440-2 Fab heavy chain × 1 445-3 Fab heavy chain × 1 445-3 Fab light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.24 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 5
Chains and sequence ranges Author chain D; PDBConstruct 1–279; UniProt 22–300

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 9d6f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9d6f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9d6f
Deposition date deposition_date2024-08-15
Structure title titleCryo-EM structure of E. coli FimH lectin domain bound to Fabs 440-2 and 454-3
Keywords keywordsAntigen, complex, adhesion, STRUCTURAL PROTEIN, CELL ADHESION, SUGAR BINDING PROTEIN; CELL ADHESION,SUGAR BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.18
Radius of gyration Rg (electron density) rg_electron31.80
Forward intensity I(0) i071071000.00
Molecular weight molecular_weight66202.0 kDa
Excluded volume excluded_volume82659 ų
Envelope volume envelope_volume114940 ų
Hydration-shell volume shell_volume31290 ų
Envelope diameter envelope_diameter109.2
Shell Rg shell_rg37.36
Envelope Rg envelope_rg31.70
Shape Rg shape_rg31.73
Total Rg total_rg32.56
Total atoms total_atoms4672
Residues n_residues610
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 dmax105.3
Rg (real space) rg_real32.31
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real7.1070e+07
I(0) uncertainty (real space) i0_real_error1.1390e+06
Rg (reciprocal space) rg_reciprocal32.26
I(0) (reciprocal space) i0_reciprocal71070000.0000
Solution quality estimate total_estimate0.8839
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.1
Skewness Skewness skewness0.347
Kurtosis Kurtosis kurtosis-0.653
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19170000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.899; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)