8v93

Cryo-EM structure of E. coli FimH lectin domain bound to Fabs 329-2 and 454-3

Method: ELECTRON MICROSCOPY Dmax: 105.6 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 Fab 454-3 heavy chain × 1 Fab 329-2 heavy chain × 1 Fab 454-3 light chain × 1 Fab 329-2 light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.12 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 4
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 Fab 454-3 heavy chain × 1 Fab 329-2 heavy chain × 1 Fab 454-3 light chain × 1 Fab 329-2 light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.12 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 4
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 8v93

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8v93
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8v93
Deposition date deposition_date2023-12-07
Structure title titleCryo-EM structure of E. coli FimH lectin domain bound to Fabs 329-2 and 454-3
Keywords keywordsBacterial proteins, lectin domain, Fab, urinary tract infections, 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_guinier31.50
Radius of gyration Rg (electron density) rg_electron31.35
Forward intensity I(0) i071349900.00
Molecular weight molecular_weight66390.0 kDa
Excluded volume excluded_volume82801 ų
Envelope volume envelope_volume105950 ų
Hydration-shell volume shell_volume30216 ų
Envelope diameter envelope_diameter111.9
Shell Rg shell_rg36.07
Envelope Rg envelope_rg31.51
Shape Rg shape_rg31.28
Total Rg total_rg32.01
Total atoms total_atoms4686
Residues n_residues614
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 dmax105.6
Rg (real space) rg_real31.78
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real7.1350e+07
I(0) uncertainty (real space) i0_real_error1.1550e+06
Rg (reciprocal space) rg_reciprocal31.66
I(0) (reciprocal space) i0_reciprocal71340000.0000
Solution quality estimate total_estimate0.8469
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.6
Skewness Skewness skewness0.496
Kurtosis Kurtosis kurtosis-0.461
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15910000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.784; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.834; Smooth: 0.821

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)