7szo

Structure of a bacterial fimbrial tip containing FocH

Method: X-RAY DIFFRACTION Dmax: 214.5 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 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 37–241 Not recorded FimF protein × 2 (A0A1M0WRP3) FimG × 1 (A8HPB0) FimH,F1C putative fimbrial adhesin fusion × 1 (Q9F6Z7,A8KI79) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.6 M POTASSIUM CHLORIDE, 0.1 M REMARK 280 SODIUM CITRATE, PH 4.1 Resolution 2.80 Å R-free 0.274
2 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain I; UniProt 37–241 Not recorded FimF protein × 2 (A0A1M0WRP3) FimG × 1 (A8HPB0) FimH,F1C putative fimbrial adhesin fusion × 1 (Q9F6Z7,A8KI79) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.6 M POTASSIUM CHLORIDE, 0.1 M REMARK 280 SODIUM CITRATE, PH 4.1 Resolution 2.80 Å R-free 0.274

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 55 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 C; PDBConstruct 1–205; UniProt 37–241 Author chain I; PDBConstruct 1–205; UniProt 37–241

FimF protein

Escherichia coli

UniProt A0A1M0WRP3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 23–176 Chain F; UniProt 23–176 Not recorded Chaperone protein FimC × 1 (P31697) FimG × 1 (A8HPB0) FimH,F1C putative fimbrial adhesin fusion × 1 (Q9F6Z7,A8KI79) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.6 M POTASSIUM CHLORIDE, 0.1 M REMARK 280 SODIUM CITRATE, PH 4.1 Resolution 2.80 Å R-free 0.274
2 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain K; UniProt 23–176 Chain L; UniProt 23–176 Not recorded Chaperone protein FimC × 1 (P31697) FimG × 1 (A8HPB0) FimH,F1C putative fimbrial adhesin fusion × 1 (Q9F6Z7,A8KI79) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.6 M POTASSIUM CHLORIDE, 0.1 M REMARK 280 SODIUM CITRATE, PH 4.1 Resolution 2.80 Å R-free 0.274

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A1M0WRP3_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–154; UniProt 23–176 Author chain F; PDBConstruct 1–154; UniProt 23–176 Author chain K; PDBConstruct 1–154; UniProt 23–176 Author chain L; PDBConstruct 1–154; UniProt 23–176

FimG

Escherichia coli

UniProt A8HPB0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 26–169 Not recorded Chaperone protein FimC × 1 (P31697) FimF protein × 2 (A0A1M0WRP3) FimH,F1C putative fimbrial adhesin fusion × 1 (Q9F6Z7,A8KI79) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.6 M POTASSIUM CHLORIDE, 0.1 M REMARK 280 SODIUM CITRATE, PH 4.1 Resolution 2.80 Å R-free 0.274
2 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain M; UniProt 26–169 Not recorded Chaperone protein FimC × 1 (P31697) FimF protein × 2 (A0A1M0WRP3) FimH,F1C putative fimbrial adhesin fusion × 1 (Q9F6Z7,A8KI79) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.6 M POTASSIUM CHLORIDE, 0.1 M REMARK 280 SODIUM CITRATE, PH 4.1 Resolution 2.80 Å R-free 0.274

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A8HPB0_ECOLX
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–144; UniProt 26–169 Author chain M; PDBConstruct 1–144; UniProt 26–169

FimH,F1C putative fimbrial adhesin fusion

Escherichia coli

UniProt A8KI79

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 243–258 Not recorded Chaperone protein FimC × 1 (P31697) FimF protein × 2 (A0A1M0WRP3) FimG × 1 (A8HPB0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.6 M POTASSIUM CHLORIDE, 0.1 M REMARK 280 SODIUM CITRATE, PH 4.1 Resolution 2.80 Å R-free 0.274
2 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain N; UniProt 243–258 Not recorded Chaperone protein FimC × 1 (P31697) FimF protein × 2 (A0A1M0WRP3) FimG × 1 (A8HPB0) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.6 M POTASSIUM CHLORIDE, 0.1 M REMARK 280 SODIUM CITRATE, PH 4.1 Resolution 2.80 Å R-free 0.274

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A8KI79_ECOLX
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 186–201; UniProt 243–258 Author chain N; PDBConstruct 186–201; UniProt 243–258

FimH,F1C putative fimbrial adhesin fusion

Escherichia coli

UniProt Q9F6Z7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 22–206 Chain H; UniProt 223–300 Not recorded Chaperone protein FimC × 1 (P31697) FimF protein × 2 (A0A1M0WRP3) FimG × 1 (A8HPB0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.6 M POTASSIUM CHLORIDE, 0.1 M REMARK 280 SODIUM CITRATE, PH 4.1 Resolution 2.80 Å R-free 0.274
2 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain N; UniProt 22–206 Chain N; UniProt 223–300 Not recorded Chaperone protein FimC × 1 (P31697) FimF protein × 2 (A0A1M0WRP3) FimG × 1 (A8HPB0) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.6 M POTASSIUM CHLORIDE, 0.1 M REMARK 280 SODIUM CITRATE, PH 4.1 Resolution 2.80 Å R-free 0.274

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q9F6Z7_ECOLX
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–185; UniProt 22–206 Author chain H; PDBConstruct 202–279; UniProt 223–300 Author chain N; PDBConstruct 1–185; UniProt 22–206 Author chain N; PDBConstruct 202–279; UniProt 223–300

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 7szo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7szo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7szo
Deposition date deposition_date2021-11-29
Structure title titleStructure of a bacterial fimbrial tip containing FocH
Keywords keywordsFIMBRIA, CELL ADHESION, FOCH; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier71.29
Radius of gyration Rg (electron density) rg_electron72.19
Forward intensity I(0) i0558962000.00
Molecular weight molecular_weight196260.0 kDa
Excluded volume excluded_volume245040 ų
Envelope volume envelope_volume421840 ų
Hydration-shell volume shell_volume55161 ų
Envelope diameter envelope_diameter237.6
Shell Rg shell_rg57.20
Envelope Rg envelope_rg68.84
Shape Rg shape_rg72.22
Total Rg total_rg71.74
Total atoms total_atoms13815
Residues n_residues1858
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 dmax214.5
Rg (real space) rg_real71.61
Rg uncertainty (real space) rg_real_error1.55
I(0) (real space) i0_real5.5840e+08
I(0) uncertainty (real space) i0_real_error1.1890e+07
Rg (reciprocal space) rg_reciprocal69.42
I(0) (reciprocal space) i0_reciprocal556400000.0000
Solution quality estimate total_estimate0.8058
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary78.0
Skewness Skewness skewness0.382
Kurtosis Kurtosis kurtosis-0.703
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0182
Highest regularization parameter α highest_alpha15530000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.800; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)