9vkv

Cryo-EM structure of the type I pilus from Escherichia Coli and the surrounding water network

Method: ELECTRON MICROSCOPY Dmax: 141.0 Å Quality: GOOD

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

Type-1 fimbrial protein, A chain

OrganismNot specified

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 24–182 Chain B; UniProt 24–182 Chain C; UniProt 24–182 Chain D; UniProt 24–182 Chain E; UniProt 24–182 Chain F; UniProt 24–182 Chain G; UniProt 24–182 Chain H; UniProt 24–182 Chain I; UniProt 24–182 Chain J; UniProt 24–182 Chain K; UniProt 24–182 Chain L; UniProt 24–182 Chain M; UniProt 24–182 Chain N; UniProt 24–182 Chain O; UniProt 24–182 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 2.09 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 1–159; UniProt 24–182 Author chain B; PDBConstruct 1–159; UniProt 24–182 Author chain C; PDBConstruct 1–159; UniProt 24–182 Author chain D; PDBConstruct 1–159; UniProt 24–182 Author chain E; PDBConstruct 1–159; UniProt 24–182 Author chain F; PDBConstruct 1–159; UniProt 24–182 Author chain G; PDBConstruct 1–159; UniProt 24–182 Author chain H; PDBConstruct 1–159; UniProt 24–182 Author chain I; PDBConstruct 1–159; UniProt 24–182 Author chain J; PDBConstruct 1–159; UniProt 24–182 Author chain K; PDBConstruct 1–159; UniProt 24–182 Author chain L; PDBConstruct 1–159; UniProt 24–182 Author chain M; PDBConstruct 1–159; UniProt 24–182 Author chain N; PDBConstruct 1–159; UniProt 24–182 Author chain O; PDBConstruct 1–159; UniProt 24–182

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 9vkv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9vkv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9vkv
Deposition date deposition_date2025-06-24
Structure title titleCryo-EM structure of the type I pilus from Escherichia Coli and the surrounding water network
Keywords keywordsType-I pilus rod, CELL ADHESION; CELL ADHESION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.08
Radius of gyration Rg (electron density) rg_electron41.77
Forward intensity I(0) i0931705000.00
Molecular weight molecular_weight237340.0 kDa
Excluded volume excluded_volume291450 ų
Envelope volume envelope_volume380720 ų
Hydration-shell volume shell_volume75349 ų
Envelope diameter envelope_diameter146.0
Shell Rg shell_rg47.35
Envelope Rg envelope_rg41.60
Shape Rg shape_rg41.75
Total Rg total_rg42.07
Total atoms total_atoms16695
Residues n_residues2385
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 dmax141.0
Rg (real space) rg_real42.14
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real9.3170e+08
I(0) uncertainty (real space) i0_real_error1.6880e+07
Rg (reciprocal space) rg_reciprocal42.08
I(0) (reciprocal space) i0_reciprocal931600000.0000
Solution quality estimate total_estimate0.8473
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.2
Skewness Skewness skewness0.473
Kurtosis Kurtosis kurtosis-0.151
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha171200000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.725; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.840

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)