4x50

Crystal structure of FimH in complex with biphenyl alpha-D-mannopyranoside

Method: X-RAY DIFFRACTION Dmax: 73.5 Å Quality: EXCELLENT

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

Protein FimH

Escherichia coli K-12

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 22–180 Not recorded 3X8 biphenyl-4-yl alpha-D-mannopyranoside × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;19% PEG 8000, 0.2 M (NH4)2SO4, 0.1 M HEPES pH 7.0. Resolution 2.00 Å R-free 0.202
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 22–180 Not recorded 3X8 biphenyl-4-yl alpha-D-mannopyranoside × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;19% PEG 8000, 0.2 M (NH4)2SO4, 0.1 M HEPES pH 7.0. Resolution 2.00 Å R-free 0.202

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 1–159; UniProt 22–180 Author chain B; PDBConstruct 1–159; UniProt 22–180

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 4x50

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4x50
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4x50
Deposition date deposition_date2014-12-04
Structure title titleCrystal structure of FimH in complex with biphenyl alpha-D-mannopyranoside
Keywords keywordssugar Binding Protein, Bacterial Adhesin, Pilus, UPEC, Antagonist Complex; SUGAR BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.12
Radius of gyration Rg (electron density) rg_electron22.26
Forward intensity I(0) i019355600.00
Molecular weight molecular_weight34445.0 kDa
Excluded volume excluded_volume43365 ų
Envelope volume envelope_volume51867 ų
Hydration-shell volume shell_volume19785 ų
Envelope diameter envelope_diameter75.5
Shell Rg shell_rg28.54
Envelope Rg envelope_rg22.02
Shape Rg shape_rg22.25
Total Rg total_rg23.08
Total atoms total_atoms4806
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 dmax73.5
Rg (real space) rg_real23.05
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real1.9360e+07
I(0) uncertainty (real space) i0_real_error2.5060e+05
Rg (reciprocal space) rg_reciprocal23.07
I(0) (reciprocal space) i0_reciprocal19360000.0000
Solution quality estimate total_estimate0.9074
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.5
Skewness Skewness skewness0.144
Kurtosis Kurtosis kurtosis-0.662
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3746000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.992

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_idd4x50a_
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_idd4x50b_
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_id4x50A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id4x50B00
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)