3sqb

Structure of the major type 1 pilus subunit FimA bound to the FimC chaperone

Method: X-RAY DIFFRACTION Dmax: 126.2 Å Quality: GOOD

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

Chaperone protein fimC

Escherichia coli

UniProt P31697

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 37–241 Fragment:UNP residues 37-241 Type-1 fimbrial protein, A chain × 1 (P04128) PEG DI(HYDROXYETHYL)ETHER × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.20 Å R-free 0.300
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 37–241 Fragment:UNP residues 37-241 Type-1 fimbrial protein, A chain × 1 (P04128) EDO 1,2-ETHANEDIOL × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.20 Å R-free 0.300
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 37–241 Fragment:UNP residues 37-241 Type-1 fimbrial protein, A chain × 1 (P04128) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.20 Å R-free 0.300
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 37–241 Fragment:UNP residues 37-241 Type-1 fimbrial protein, A chain × 1 (P04128) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.20 Å R-free 0.300

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.

22 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMC_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–205; UniProt 37–241 Author chain C; PDBConstruct 1–205; UniProt 37–241 Author chain E; PDBConstruct 1–205; UniProt 37–241 Author chain G; PDBConstruct 1–205; UniProt 37–241

Type-1 fimbrial protein, A chain

Escherichia coli

UniProt P04128

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 37–182 Fragment:UNP residues 37-182 Chaperone protein fimC × 1 (P31697) PEG DI(HYDROXYETHYL)ETHER × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.20 Å R-free 0.300
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 37–182 Fragment:UNP residues 37-182 Chaperone protein fimC × 1 (P31697) EDO 1,2-ETHANEDIOL × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.20 Å R-free 0.300
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 37–182 Fragment:UNP residues 37-182 Chaperone protein fimC × 1 (P31697) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.20 Å R-free 0.300
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 37–182 Fragment:UNP residues 37-182 Chaperone protein fimC × 1 (P31697) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.20 Å R-free 0.300

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.

20 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMA1_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 7–152; UniProt 37–182 Author chain D; PDBConstruct 7–152; UniProt 37–182 Author chain F; PDBConstruct 7–152; UniProt 37–182 Author chain H; PDBConstruct 7–152; UniProt 37–182

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 3sqb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3sqb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3sqb
Deposition date deposition_date2011-07-05
Structure title titleStructure of the major type 1 pilus subunit FimA bound to the FimC chaperone
Keywords keywordsimmunoglobin-like fold, involved in type 1 pilus assembly, STRUCTURAL PROTEIN-CHAPERONE complex; STRUCTURAL PROTEIN/CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.82
Radius of gyration Rg (electron density) rg_electron38.18
Forward intensity I(0) i0200429000.00
Molecular weight molecular_weight110620.0 kDa
Excluded volume excluded_volume137000 ų
Envelope volume envelope_volume207510 ų
Hydration-shell volume shell_volume46723 ų
Envelope diameter envelope_diameter133.4
Shell Rg shell_rg42.49
Envelope Rg envelope_rg37.75
Shape Rg shape_rg38.20
Total Rg total_rg38.40
Total atoms total_atoms7792
Residues n_residues1100
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 dmax126.2
Rg (real space) rg_real38.79
Rg uncertainty (real space) rg_real_error0.97
I(0) (real space) i0_real2.0040e+08
I(0) uncertainty (real space) i0_real_error3.4940e+06
Rg (reciprocal space) rg_reciprocal38.82
I(0) (reciprocal space) i0_reciprocal200400000.0000
Solution quality estimate total_estimate0.8826
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.2
Skewness Skewness skewness0.278
Kurtosis Kurtosis kurtosis-0.325
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15860000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.817

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id3sqbA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3sqbA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3sqbB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id3sqbC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3sqbC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3sqbD00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id3sqbE01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3sqbE02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)