7b0x

Crystal structure of the ternary complex of the E. coli type 1 pilus proteins FimC, FimI and the N-terminal domain of FimD

Method: X-RAY DIFFRACTION Dmax: 93.0 Å Quality: GOOD

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

Chaperone protein FimC

Escherichia coli (strain K12)

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 Fimbrin-like protein FimI × 1 (P39264) Outer membrane usher protein FimD × 1 (P30130) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M Hepes pH 8.4, 15 % PEG 4000 Resolution 1.70 Å R-free 0.252

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

Fimbrin-like protein FimI

Escherichia coli (strain K12)

UniProt P39264

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 I; UniProt 40–179 Not recorded Chaperone protein FimC × 1 (P31697) Outer membrane usher protein FimD × 1 (P30130) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M Hepes pH 8.4, 15 % PEG 4000 Resolution 1.70 Å R-free 0.252

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMI_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–140; UniProt 40–179

Outer membrane usher protein FimD

Escherichia coli (strain K12)

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 Not recorded Chaperone protein FimC × 1 (P31697) Fimbrin-like protein FimI × 1 (P39264) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M Hepes pH 8.4, 15 % PEG 4000 Resolution 1.70 Å R-free 0.252

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 3
Chains and sequence ranges Author chain D; PDBConstruct 1–125; UniProt 46–170

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 7b0x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7b0x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7b0x
Deposition date deposition_date2020-11-23
Structure title titleCrystal structure of the ternary complex of the E. coli type 1 pilus proteins FimC, FimI and the N-terminal domain of FimD
Keywords keywordsstructural protein complex, pilus assembly, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.75
Radius of gyration Rg (electron density) rg_electron26.70
Forward intensity I(0) i045154800.00
Molecular weight molecular_weight51212.0 kDa
Excluded volume excluded_volume63786 ų
Envelope volume envelope_volume80572 ų
Hydration-shell volume shell_volume26628 ų
Envelope diameter envelope_diameter98.3
Shell Rg shell_rg32.14
Envelope Rg envelope_rg27.21
Shape Rg shape_rg26.68
Total Rg total_rg27.37
Total atoms total_atoms3600
Residues n_residues467
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 dmax93.0
Rg (real space) rg_real27.83
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real4.5150e+07
I(0) uncertainty (real space) i0_real_error7.7150e+05
Rg (reciprocal space) rg_reciprocal27.81
I(0) (reciprocal space) i0_reciprocal45150000.0000
Solution quality estimate total_estimate0.8881
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.4
Skewness Skewness skewness0.372
Kurtosis Kurtosis kurtosis-0.411
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha9018000.0000
Real-space data points n_real_points58
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: 0.930; Smooth: 0.959

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7b0xI01
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)