1uwf

1.7 A resolution structure of the receptor binding domain of the FimH adhesin from uropathogenic E. coli

Method: X-RAY DIFFRACTION Dmax: 68.5 Å Quality: REASONABLE

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

FIMH PROTEIN

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 22–179 Fragment:N-TERMINAL LECTIN DOMAIN, RESIDUES 22-179 DEG butyl alpha-D-mannopyranoside × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;1.1 MM PROTEIN, 0.1 M HEPES PH 7.5, 10 % PEG6000, 5% V/V MPD Resolution 1.69 Å R-free 0.218

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 1–158; UniProt 22–179

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 1uwf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1uwf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1uwf
Deposition date deposition_date2004-02-05
Structure title title1.7 A resolution structure of the receptor binding domain of the FimH adhesin from uropathogenic E. coli
Keywords keywordsBACTERIAL ADHESIN, CARBOHYDRATE RECOGNITION, ADHERENCE TO MAMMALIAN CELLS, IG-VARIABLE FOLD, CELL ADHESION; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.47
Radius of gyration Rg (electron density) rg_electron16.53
Forward intensity I(0) i05430320.00
Molecular weight molecular_weight17235.0 kDa
Excluded volume excluded_volume21681 ų
Envelope volume envelope_volume23866 ų
Hydration-shell volume shell_volume13056 ų
Envelope diameter envelope_diameter67.0
Shell Rg shell_rg21.52
Envelope Rg envelope_rg17.02
Shape Rg shape_rg16.50
Total Rg total_rg17.51
Total atoms total_atoms1218
Residues n_residues158
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 dmax68.5
Rg (real space) rg_real17.58
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real5.4300e+06
I(0) uncertainty (real space) i0_real_error7.1330e+04
Rg (reciprocal space) rg_reciprocal17.57
I(0) (reciprocal space) i0_reciprocal5430000.0000
Solution quality estimate total_estimate0.6888
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.3
Skewness Skewness skewness0.560
Kurtosis Kurtosis kurtosis0.080
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1311000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.475; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.527; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1uwfa_
Class classb — All beta proteins
Fold Fold foldb.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamilyb.2.3 — Bacterial adhesins
Family Family familyb.2.3.2 — Pilus subunits

CATH v4.4 (1 domains)

Domain ID domain_id1uwfA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain

8. Citations (1)

9. Files and Curves (10)