3bwu

Crystal structure of the ternary complex of FimD (N-Terminal Domain, FimDN) with FimC and the N-terminally truncated pilus subunit FimF (FimFt)

Method: X-RAY DIFFRACTION Dmax: 87.1 Å Quality: REASONABLE

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 37–241 Not recorded Outer membrane usher protein FimD, N-terminal domain × 1 (P30130) Protein fimF × 1 (P08189) EDO 1,2-ETHANEDIOL × 13 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;20 mM Tris/HCl pH 8.0, 20% PEG 8000, 50 mM succinic acid pH 4.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.76 Å R-free 0.212

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 56 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

Outer membrane usher protein FimD, N-terminal domain

Escherichia coli

UniProt P30130

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 46–170 Fragment:N-terminal domain, Residues 1-125 Chaperone protein fimC × 1 (P31697) Protein fimF × 1 (P08189) EDO 1,2-ETHANEDIOL × 13 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;20 mM Tris/HCl pH 8.0, 20% PEG 8000, 50 mM succinic acid pH 4.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.76 Å R-free 0.212

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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMD_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–125; UniProt 46–170

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 35–176 Fragment:N-terminal truncation construct of pilus subunit fimF, Residues 13-154 Chaperone protein fimC × 1 (P31697) Outer membrane usher protein FimD, N-terminal domain × 1 (P30130) EDO 1,2-ETHANEDIOL × 13 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;20 mM Tris/HCl pH 8.0, 20% PEG 8000, 50 mM succinic acid pH 4.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.76 Å R-free 0.212

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 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMF_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain F; PDBConstruct 1–142; UniProt 35–176

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 3bwu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3bwu
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3bwu
Deposition date deposition_date2008-01-10
Structure title titleCrystal structure of the ternary complex of FimD (N-Terminal Domain, FimDN) with FimC and the N-terminally truncated pilus subunit FimF (FimFt)
Keywords keywords;Usher, N-terminal domain, ternary complex with chaperone and pilus subunit, CHAPERONE, STRUCTURAL PROTEIN, MEBRANE PROTEIN, STRUCTURAL, MEMBRANE PROTEIN ;; CHAPERONE, STRUCTURAL, MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.38
Radius of gyration Rg (electron density) rg_electron25.50
Forward intensity I(0) i040760600.00
Molecular weight molecular_weight49257.0 kDa
Excluded volume excluded_volume61673 ų
Envelope volume envelope_volume75670 ų
Hydration-shell volume shell_volume25964 ų
Envelope diameter envelope_diameter90.3
Shell Rg shell_rg31.45
Envelope Rg envelope_rg25.80
Shape Rg shape_rg25.45
Total Rg total_rg26.32
Total atoms total_atoms3456
Residues n_residues449
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 dmax87.1
Rg (real space) rg_real26.42
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real4.0760e+07
I(0) uncertainty (real space) i0_real_error5.9530e+05
Rg (reciprocal space) rg_reciprocal26.41
I(0) (reciprocal space) i0_reciprocal40760000.0000
Solution quality estimate total_estimate0.7253
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.1
Skewness Skewness skewness0.378
Kurtosis Kurtosis kurtosis-0.328
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8491000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 0.291; Positv: 1.000; Valcen: 0.954; Smooth: 0.923

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3bwuc1
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_idd3bwuc2
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_idd3bwud_
Class classb — All beta proteins
Fold Fold foldb.167 — FimD N-terminal domain-like
Superfamily Superfamily superfamilyb.167.1 — FimD N-terminal domain-like
Family Family familyb.167.1.1 — Usher N-domain

CATH v4.4 (4 domains)

Domain ID domain_id3bwuC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3bwuC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3bwuD00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily410 — PapC, N-terminal domain
Domain ID domain_id3bwuF00
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)