8psv

2.7 A cryo-EM structure of in vitro assembled type 1 pilus rod

Method: ELECTRON MICROSCOPY Dmax: 86.5 Å Quality: GOOD

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

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 homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–182 Chain B; UniProt 1–182 Chain C; UniProt 1–182 Chain D; UniProt 1–182 Chain E; UniProt 1–182 Chain F; UniProt 1–182 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7;in ddH2O. cryo-EM vitrification conditions:Cryogen ETHANE;3 ul sample, 30 s wait time, 0.5 s drain time, 6 s blotting Resolution 2.70 Å

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 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMA1_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–182; UniProt 1–182 Author chain B; PDBConstruct 1–182; UniProt 1–182 Author chain C; PDBConstruct 1–182; UniProt 1–182 Author chain D; PDBConstruct 1–182; UniProt 1–182 Author chain E; PDBConstruct 1–182; UniProt 1–182 Author chain F; PDBConstruct 1–182; UniProt 1–182

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 8psv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8psv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8psv
Deposition date deposition_date2023-07-13
Structure title title2.7 A cryo-EM structure of in vitro assembled type 1 pilus rod
Keywords keywords;FimA, pilus, monomer, subunit, pili, main structural subunit, high resolution, STRUCTURAL PROTEIN, cryo-EM, helical processing, RELION, Chaperone-usher pilus ;; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.55
Radius of gyration Rg (electron density) rg_electron28.34
Forward intensity I(0) i0159882000.00
Molecular weight molecular_weight94406.0 kDa
Excluded volume excluded_volume115970 ų
Envelope volume envelope_volume150840 ų
Hydration-shell volume shell_volume42690 ų
Envelope diameter envelope_diameter91.8
Shell Rg shell_rg37.06
Envelope Rg envelope_rg27.72
Shape Rg shape_rg28.31
Total Rg total_rg29.21
Total atoms total_atoms6642
Residues n_residues948
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 dmax86.5
Rg (real space) rg_real29.32
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real1.5990e+08
I(0) uncertainty (real space) i0_real_error2.1870e+06
Rg (reciprocal space) rg_reciprocal29.42
I(0) (reciprocal space) i0_reciprocal159900000.0000
Solution quality estimate total_estimate0.8994
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.1
Skewness Skewness skewness-0.008
Kurtosis Kurtosis kurtosis-0.561
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36130000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.883

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)