5l4y

Crystal structure of FimH lectin domain in complex with 4-Fluoro-Heptylmannoside

Method: X-RAY DIFFRACTION Dmax: 73.2 Å Quality: GOOD

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

Protein FimH

Escherichia coli (strain K12)

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 Not recorded 6K3 heptyl 4-deoxy-4-fluoro-alpha-D-mannopyranoside × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;285 K;0.2 M (NH4)2SO4, 0.1 M Hepes pH 7 and 25-30% PEG3350 Resolution 1.90 Å R-free 0.229
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 22–179 Not recorded 6K3 heptyl 4-deoxy-4-fluoro-alpha-D-mannopyranoside × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;285 K;0.2 M (NH4)2SO4, 0.1 M Hepes pH 7 and 25-30% PEG3350 Resolution 1.90 Å R-free 0.229

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 137 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 Author chain B; 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 5l4y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5l4y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5l4y
Deposition date deposition_date2016-05-26
Structure title titleCrystal structure of FimH lectin domain in complex with 4-Fluoro-Heptylmannoside
Keywords keywordsFimH, Type 1 pilus, urinary tract infection, UTI, carbohydrate, lectin, mannose, cell adhesion, sugar binding protein; SUGAR BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.04
Radius of gyration Rg (electron density) rg_electron22.17
Forward intensity I(0) i019298300.00
Molecular weight molecular_weight34375.0 kDa
Excluded volume excluded_volume43284 ų
Envelope volume envelope_volume51709 ų
Hydration-shell volume shell_volume19818 ų
Envelope diameter envelope_diameter75.9
Shell Rg shell_rg28.39
Envelope Rg envelope_rg21.95
Shape Rg shape_rg22.15
Total Rg total_rg23.03
Total atoms total_atoms2430
Residues n_residues316
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 dmax73.2
Rg (real space) rg_real22.98
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real1.9300e+07
I(0) uncertainty (real space) i0_real_error2.3720e+05
Rg (reciprocal space) rg_reciprocal23.00
I(0) (reciprocal space) i0_reciprocal19300000.0000
Solution quality estimate total_estimate0.8277
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary30.4
Skewness Skewness skewness0.149
Kurtosis Kurtosis kurtosis-0.643
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3644000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5l4ya_
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
Domain ID domain_idd5l4yb_
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 (2 domains)

Domain ID domain_id5l4yA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id5l4yB00
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)