3zl1

A thiazolyl-mannoside bound to FimH, monoclinic space group

Method: X-RAY DIFFRACTION Dmax: 86.3 Å Quality: GOOD

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

PROTEIN FIMH

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:LECTIN DOMAIN OR RECEPTOR BINDING DOMAIN, RESIDUES 22-179 BWG N-{5-[(1R)-1-hydroxyethyl]-1,3-thiazol-2-yl}-alpha-D-mannopyranosylamine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.1 M NACL, 0.1 M TRIS PH 7.5, 11 % (W/V) PEG 4000 Resolution 1.55 Å R-free 0.262
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 22–179 Fragment:LECTIN DOMAIN OR RECEPTOR BINDING DOMAIN, RESIDUES 22-179 BWG N-{5-[(1R)-1-hydroxyethyl]-1,3-thiazol-2-yl}-alpha-D-mannopyranosylamine × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.1 M NACL, 0.1 M TRIS PH 7.5, 11 % (W/V) PEG 4000 Resolution 1.55 Å R-free 0.262

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 3zl1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3zl1
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3zl1
Deposition date deposition_date2013-01-27
Structure title titleA thiazolyl-mannoside bound to FimH, monoclinic space group
Keywords keywords;CELL ADHESION, TYPE-1 FIMBRIAE, THIAZOLE, CROHN'S DISEASE, IMMUNOGLOBULIN ;; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.56
Radius of gyration Rg (electron density) rg_electron23.75
Forward intensity I(0) i019994400.00
Molecular weight molecular_weight34458.0 kDa
Excluded volume excluded_volume43193 ų
Envelope volume envelope_volume50033 ų
Hydration-shell volume shell_volume19314 ų
Envelope diameter envelope_diameter88.6
Shell Rg shell_rg28.50
Envelope Rg envelope_rg23.73
Shape Rg shape_rg23.76
Total Rg total_rg24.32
Total atoms total_atoms2433
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 dmax86.3
Rg (real space) rg_real24.82
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.9990e+07
I(0) uncertainty (real space) i0_real_error2.8530e+05
Rg (reciprocal space) rg_reciprocal24.76
I(0) (reciprocal space) i0_reciprocal19990000.0000
Solution quality estimate total_estimate0.8337
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.550
Kurtosis Kurtosis kurtosis-0.216
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3544000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.753; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.595; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3zl1a_
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_idd3zl1b_
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_id3zl1A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id3zl1B00
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)