3jwn

Complex of FimC, FimF, FimG and FimH

Method: X-RAY DIFFRACTION Dmax: 212.5 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 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 37–241 Not recorded Protein fimF × 2 (P08189) Protein fimG × 1 (P08190) FimH protein × 1 (Q0T8Y8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.1;293 K;1.6 M potassium chloride, 0.1 M sodium citrate, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.69 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain I; UniProt 37–241 Not recorded Protein fimF × 2 (P08189) Protein fimG × 1 (P08190) FimH protein × 1 (Q0T8Y8) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.1;293 K;1.6 M potassium chloride, 0.1 M sodium citrate, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.69 Å R-free 0.272

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

Protein fimF

Escherichia coli

UniProt P08189

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 23–176 Chain F; UniProt 23–176 Fragment:UNP residues 23-176 Chaperone protein fimC × 1 (P31697) Protein fimG × 1 (P08190) FimH protein × 1 (Q0T8Y8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.1;293 K;1.6 M potassium chloride, 0.1 M sodium citrate, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.69 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain K; UniProt 23–176 Chain L; UniProt 23–176 Fragment:UNP residues 23-176 Chaperone protein fimC × 1 (P31697) Protein fimG × 1 (P08190) FimH protein × 1 (Q0T8Y8) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.1;293 K;1.6 M potassium chloride, 0.1 M sodium citrate, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.69 Å R-free 0.272

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.

13 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMF_ECOLI
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

Protein fimG

Escherichia coli

UniProt P08190

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 24–167 Not recorded Chaperone protein fimC × 1 (P31697) Protein fimF × 2 (P08189) FimH protein × 1 (Q0T8Y8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.1;293 K;1.6 M potassium chloride, 0.1 M sodium citrate, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.69 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain M; UniProt 24–167 Not recorded Chaperone protein fimC × 1 (P31697) Protein fimF × 2 (P08189) FimH protein × 1 (Q0T8Y8) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.1;293 K;1.6 M potassium chloride, 0.1 M sodium citrate, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.69 Å R-free 0.272

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.

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

View Construct and Data Evidence
UniProt name FIMG_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–144; UniProt 24–167 Author chain M; PDBConstruct 1–144; UniProt 24–167

FimH protein

Escherichia coli

UniProt Q0T8Y8

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 25–303 Fragment:UNP residues 25-303 Chaperone protein fimC × 1 (P31697) Protein fimF × 2 (P08189) Protein fimG × 1 (P08190) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.1;293 K;1.6 M potassium chloride, 0.1 M sodium citrate, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.69 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain N; UniProt 25–303 Fragment:UNP residues 25-303 Chaperone protein fimC × 1 (P31697) Protein fimF × 2 (P08189) Protein fimG × 1 (P08190) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.1;293 K;1.6 M potassium chloride, 0.1 M sodium citrate, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.69 Å R-free 0.272

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.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q0T8Y8_ECOL5
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–279; UniProt 25–303 Author chain N; PDBConstruct 1–279; UniProt 25–303

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 3jwn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3jwn
Deposition date deposition_date2009-09-18
Structure title titleComplex of FimC, FimF, FimG and FimH
Keywords keywords;fimbria, cell adhesion, fimh, fimc, fimf, fimg, chaperone, fibrium, immunoglobulin domain, Fimbrium, Periplasm, Disulfide bond, protein binding-cell adhesion COMPLEX ;; protein binding/cell adhesion
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier71.41
Radius of gyration Rg (electron density) rg_electron72.32
Forward intensity I(0) i0558137000.00
Molecular weight molecular_weight196520.0 kDa
Excluded volume excluded_volume245470 ų
Envelope volume envelope_volume429290 ų
Hydration-shell volume shell_volume55697 ų
Envelope diameter envelope_diameter236.8
Shell Rg shell_rg57.80
Envelope Rg envelope_rg69.20
Shape Rg shape_rg72.34
Total Rg total_rg71.88
Total atoms total_atoms13834
Residues n_residues1859
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 dmax212.5
Rg (real space) rg_real71.69
Rg uncertainty (real space) rg_real_error1.60
I(0) (real space) i0_real5.5750e+08
I(0) uncertainty (real space) i0_real_error1.0880e+07
Rg (reciprocal space) rg_reciprocal69.53
I(0) (reciprocal space) i0_reciprocal555600000.0000
Solution quality estimate total_estimate0.8056
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary77.3
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.705
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0071
Highest regularization parameter α highest_alpha15460000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.793; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 26 domains

SCOP 2.08 (12 domains)

Domain ID domain_idd3jwnc1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.11 — PapD-like
Family Family familyb.1.11.1 — Pilus chaperone
Domain ID domain_idd3jwnc2
Class classb — All beta proteins
Fold Fold foldb.7 — C2 domain-like
Superfamily Superfamily superfamilyb.7.2 — Periplasmic chaperone C-domain
Family Family familyb.7.2.1 — Periplasmic chaperone C-domain
Domain ID domain_idd3jwne_
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.2.3.0 — automated matches
Domain ID domain_idd3jwnf_
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.2.3.0 — automated matches
Domain ID domain_idd3jwnh1
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_idd3jwnh2
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_idd3jwni1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.11 — PapD-like
Family Family familyb.1.11.1 — Pilus chaperone
Domain ID domain_idd3jwni2
Class classb — All beta proteins
Fold Fold foldb.7 — C2 domain-like
Superfamily Superfamily superfamilyb.7.2 — Periplasmic chaperone C-domain
Family Family familyb.7.2.1 — Periplasmic chaperone C-domain
Domain ID domain_idd3jwnk_
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.2.3.0 — automated matches
Domain ID domain_idd3jwnl_
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.2.3.0 — automated matches
Domain ID domain_idd3jwnn1
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_idd3jwnn2
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 (14 domains)

Domain ID domain_id3jwnC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3jwnC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3jwnE00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id3jwnF00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id3jwnG00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id3jwnH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id3jwnH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id3jwnI01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3jwnI02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3jwnK00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id3jwnL00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id3jwnM00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id3jwnN01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id3jwnN02
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)