8by3

FimH lectin domain in complex with oligomannose-6

Method: X-RAY DIFFRACTION Dmax: 180.5 Å Quality: REASONABLE

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

Type 1 fimbrin D-mannose specific adhesin

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 Other combination Homooligomer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 22–179 Chain C; UniProt 22–179 Not recorded ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NI NICKEL (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;1 M Lithium sulphate 100 mM Tris-HCl, pH 8.5 10 mM Nickel chloride 3% glycerol Resolution 3.19 Å R-free 0.238
2 Other combination Homooligomer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 22–179 Chain D; UniProt 22–179 Not recorded ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NI NICKEL (II) ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;1 M Lithium sulphate 100 mM Tris-HCl, pH 8.5 10 mM Nickel chloride 3% glycerol Resolution 3.19 Å R-free 0.238

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 Author chain C; PDBConstruct 1–158; UniProt 22–179 Author chain D; 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 8by3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8by3
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8by3
Deposition date deposition_date2022-12-11
Structure title titleFimH lectin domain in complex with oligomannose-6
Keywords keywordsType-1 fimbriae, Escherichia coli, FimH, Adhesin, Lectin, Oligomannose, High-mannose, 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_guinier47.46
Radius of gyration Rg (electron density) rg_electron49.21
Forward intensity I(0) i074720000.00
Molecular weight molecular_weight70863.0 kDa
Excluded volume excluded_volume88654 ų
Envelope volume envelope_volume123780 ų
Hydration-shell volume shell_volume24814 ų
Envelope diameter envelope_diameter178.1
Shell Rg shell_rg42.50
Envelope Rg envelope_rg48.96
Shape Rg shape_rg49.20
Total Rg total_rg48.91
Total atoms total_atoms4988
Residues n_residues632
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 dmax180.5
Rg (real space) rg_real48.72
Rg uncertainty (real space) rg_real_error3.43
I(0) (real space) i0_real7.4720e+07
I(0) uncertainty (real space) i0_real_error1.5190e+06
Rg (reciprocal space) rg_reciprocal47.47
I(0) (reciprocal space) i0_reciprocal74600000.0000
Solution quality estimate total_estimate0.6306
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.9
Skewness Skewness skewness0.581
Kurtosis Kurtosis kurtosis-0.496
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1953000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.134; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.069; Smooth: 0.728

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8by3A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id8by3B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id8by3C01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id8by3D01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain

8. Citations (4)

9. Files and Curves (10)