7cgb

Cryo-EM structure of the flagellar hook from Salmonella

Method: ELECTRON MICROSCOPY Dmax: 257.5 Å Quality: EXCELLENT

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

Flagellar hook protein FlgE

OrganismNot specified

UniProt P0A1J1

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain DL; UniProt 1–403 Chain DM; UniProt 1–403 Chain DN; UniProt 1–403 Chain DO; UniProt 1–403 Chain DP; UniProt 1–403 Chain DQ; UniProt 1–403 Chain DR; UniProt 1–403 Chain DS; UniProt 1–403 Chain DT; UniProt 1–403 Chain DU; UniProt 1–403 Chain DV; UniProt 1–403 Chain DW; UniProt 1–403 Chain DX; UniProt 1–403 Chain DY; UniProt 1–403 Chain DZ; UniProt 1–403 Chain EA; UniProt 1–403 Chain EB; UniProt 1–403 Chain EC; UniProt 1–403 Chain ED; UniProt 1–403 Chain EE; UniProt 1–403 Chain EF; UniProt 1–403 Chain EG; UniProt 1–403 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.40 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 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGE_SALTY
Isoform
PDB entities 1
Chains and sequence ranges Author chain DL; PDBConstruct 1–403; UniProt 1–403 Author chain DM; PDBConstruct 1–403; UniProt 1–403 Author chain DN; PDBConstruct 1–403; UniProt 1–403 Author chain DO; PDBConstruct 1–403; UniProt 1–403 Author chain DP; PDBConstruct 1–403; UniProt 1–403 Author chain DQ; PDBConstruct 1–403; UniProt 1–403 Author chain DR; PDBConstruct 1–403; UniProt 1–403 Author chain DS; PDBConstruct 1–403; UniProt 1–403 Author chain DT; PDBConstruct 1–403; UniProt 1–403 Author chain DU; PDBConstruct 1–403; UniProt 1–403 Author chain DV; PDBConstruct 1–403; UniProt 1–403 Author chain DW; PDBConstruct 1–403; UniProt 1–403 Author chain DX; PDBConstruct 1–403; UniProt 1–403 Author chain DY; PDBConstruct 1–403; UniProt 1–403 Author chain DZ; PDBConstruct 1–403; UniProt 1–403 Author chain EA; PDBConstruct 1–403; UniProt 1–403 Author chain EB; PDBConstruct 1–403; UniProt 1–403 Author chain EC; PDBConstruct 1–403; UniProt 1–403 Author chain ED; PDBConstruct 1–403; UniProt 1–403 Author chain EE; PDBConstruct 1–403; UniProt 1–403 Author chain EF; PDBConstruct 1–403; UniProt 1–403 Author chain EG; PDBConstruct 1–403; UniProt 1–403

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 7cgb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7cgb
Deposition date deposition_date2020-07-01
Structure title titleCryo-EM structure of the flagellar hook from Salmonella
Keywords keywordsHook, FlgE, Hook-basal body, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier70.58
Radius of gyration Rg (electron density) rg_electron70.20
Forward intensity I(0) i012955600000.00
Molecular weight molecular_weight921740.0 kDa
Excluded volume excluded_volume1134600 ų
Envelope volume envelope_volume1886700 ų
Hydration-shell volume shell_volume209990 ų
Envelope diameter envelope_diameter224.4
Shell Rg shell_rg81.05
Envelope Rg envelope_rg68.70
Shape Rg shape_rg70.21
Total Rg total_rg70.30
Total atoms total_atoms64834
Residues n_residues8822
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 dmax257.5
Rg (real space) rg_real73.46
Rg uncertainty (real space) rg_real_error1.51
I(0) (real space) i0_real1.2960e+10
I(0) uncertainty (real space) i0_real_error2.7520e+08
Rg (reciprocal space) rg_reciprocal71.44
I(0) (reciprocal space) i0_reciprocal12980000000.0000
Solution quality estimate total_estimate0.9011
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary93.7
Skewness Skewness skewness0.422
Kurtosis Kurtosis kurtosis0.208
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.9890
Highest regularization parameter α highest_alpha3143000000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.737; Stabil: 0.884; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)