9m7b

Structure of flagellar hook at 3.14 angstroms resolution,conformation 2.

Method: ELECTRON MICROSCOPY Dmax: 295.4 Å Quality: GOOD

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 × 66 PDB declaration: 66-meric(66) Consistent with protein copy count Chain DA; UniProt 2–403 Chain DB; UniProt 2–403 Chain DC; UniProt 2–403 Chain DD; UniProt 2–403 Chain DE; UniProt 2–403 Chain DF; UniProt 2–403 Chain DG; UniProt 2–403 Chain DH; UniProt 2–403 Chain DI; UniProt 2–403 Chain DJ; UniProt 2–403 Chain DK; UniProt 2–403 Chain EA; UniProt 2–403 Chain EB; UniProt 2–403 Chain EC; UniProt 2–403 Chain ED; UniProt 2–403 Chain EE; UniProt 2–403 Chain EF; UniProt 2–403 Chain EG; UniProt 2–403 Chain EH; UniProt 2–403 Chain EI; UniProt 2–403 Chain EJ; UniProt 2–403 Chain EK; UniProt 2–403 Chain FA; UniProt 2–403 Chain FB; UniProt 2–403 Chain FC; UniProt 2–403 Chain FD; UniProt 2–403 Chain FE; UniProt 2–403 Chain FF; UniProt 2–403 Chain FG; UniProt 2–403 Chain FH; UniProt 2–403 Chain FI; UniProt 2–403 Chain FJ; UniProt 2–403 Chain FK; UniProt 2–403 Chain GA; UniProt 2–403 Chain GB; UniProt 2–403 Chain GC; UniProt 2–403 Chain GD; UniProt 2–403 Chain GE; UniProt 2–403 Chain GF; UniProt 2–403 Chain GG; UniProt 2–403 Chain GH; UniProt 2–403 Chain GI; UniProt 2–403 Chain GJ; UniProt 2–403 Chain GK; UniProt 2–403 Chain HA; UniProt 2–403 Chain HB; UniProt 2–403 Chain HC; UniProt 2–403 Chain HD; UniProt 2–403 Chain HE; UniProt 2–403 Chain HF; UniProt 2–403 Chain HG; UniProt 2–403 Chain HH; UniProt 2–403 Chain HI; UniProt 2–403 Chain HJ; UniProt 2–403 Chain HK; UniProt 2–403 Chain IA; UniProt 2–403 Chain IB; UniProt 2–403 Chain IC; UniProt 2–403 Chain ID; UniProt 2–403 Chain IE; UniProt 2–403 Chain IF; UniProt 2–403 Chain IG; UniProt 2–403 Chain IH; UniProt 2–403 Chain II; UniProt 2–403 Chain IJ; UniProt 2–403 Chain IK; UniProt 2–403 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 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 DA; PDBConstruct 1–402; UniProt 2–403 Author chain DB; PDBConstruct 1–402; UniProt 2–403 Author chain DC; PDBConstruct 1–402; UniProt 2–403 Author chain DD; PDBConstruct 1–402; UniProt 2–403 Author chain DE; PDBConstruct 1–402; UniProt 2–403 Author chain DF; PDBConstruct 1–402; UniProt 2–403 Author chain DG; PDBConstruct 1–402; UniProt 2–403 Author chain DH; PDBConstruct 1–402; UniProt 2–403 Author chain DI; PDBConstruct 1–402; UniProt 2–403 Author chain DJ; PDBConstruct 1–402; UniProt 2–403 Author chain DK; PDBConstruct 1–402; UniProt 2–403 Author chain EA; PDBConstruct 1–402; UniProt 2–403 Author chain EB; PDBConstruct 1–402; UniProt 2–403 Author chain EC; PDBConstruct 1–402; UniProt 2–403 Author chain ED; PDBConstruct 1–402; UniProt 2–403 Author chain EE; PDBConstruct 1–402; UniProt 2–403 Author chain EF; PDBConstruct 1–402; UniProt 2–403 Author chain EG; PDBConstruct 1–402; UniProt 2–403 Author chain EH; PDBConstruct 1–402; UniProt 2–403 Author chain EI; PDBConstruct 1–402; UniProt 2–403 Author chain EJ; PDBConstruct 1–402; UniProt 2–403 Author chain EK; PDBConstruct 1–402; UniProt 2–403 Author chain FA; PDBConstruct 1–402; UniProt 2–403 Author chain FB; PDBConstruct 1–402; UniProt 2–403 Author chain FC; PDBConstruct 1–402; UniProt 2–403 Author chain FD; PDBConstruct 1–402; UniProt 2–403 Author chain FE; PDBConstruct 1–402; UniProt 2–403 Author chain FF; PDBConstruct 1–402; UniProt 2–403 Author chain FG; PDBConstruct 1–402; UniProt 2–403 Author chain FH; PDBConstruct 1–402; UniProt 2–403 Author chain FI; PDBConstruct 1–402; UniProt 2–403 Author chain FJ; PDBConstruct 1–402; UniProt 2–403 Author chain FK; PDBConstruct 1–402; UniProt 2–403 Author chain GA; PDBConstruct 1–402; UniProt 2–403 Author chain GB; PDBConstruct 1–402; UniProt 2–403 Author chain GC; PDBConstruct 1–402; UniProt 2–403 Author chain GD; PDBConstruct 1–402; UniProt 2–403 Author chain GE; PDBConstruct 1–402; UniProt 2–403 Author chain GF; PDBConstruct 1–402; UniProt 2–403 Author chain GG; PDBConstruct 1–402; UniProt 2–403 Author chain GH; PDBConstruct 1–402; UniProt 2–403 Author chain GI; PDBConstruct 1–402; UniProt 2–403 Author chain GJ; PDBConstruct 1–402; UniProt 2–403 Author chain GK; PDBConstruct 1–402; UniProt 2–403 Author chain HA; PDBConstruct 1–402; UniProt 2–403 Author chain HB; PDBConstruct 1–402; UniProt 2–403 Author chain HC; PDBConstruct 1–402; UniProt 2–403 Author chain HD; PDBConstruct 1–402; UniProt 2–403 Author chain HE; PDBConstruct 1–402; UniProt 2–403 Author chain HF; PDBConstruct 1–402; UniProt 2–403 Author chain HG; PDBConstruct 1–402; UniProt 2–403 Author chain HH; PDBConstruct 1–402; UniProt 2–403 Author chain HI; PDBConstruct 1–402; UniProt 2–403 Author chain HJ; PDBConstruct 1–402; UniProt 2–403 Author chain HK; PDBConstruct 1–402; UniProt 2–403 Author chain IA; PDBConstruct 1–402; UniProt 2–403 Author chain IB; PDBConstruct 1–402; UniProt 2–403 Author chain IC; PDBConstruct 1–402; UniProt 2–403 Author chain ID; PDBConstruct 1–402; UniProt 2–403 Author chain IE; PDBConstruct 1–402; UniProt 2–403 Author chain IF; PDBConstruct 1–402; UniProt 2–403 Author chain IG; PDBConstruct 1–402; UniProt 2–403 Author chain IH; PDBConstruct 1–402; UniProt 2–403 Author chain II; PDBConstruct 1–402; UniProt 2–403 Author chain IJ; PDBConstruct 1–402; UniProt 2–403 Author chain IK; PDBConstruct 1–402; UniProt 2–403

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 9m7b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9m7b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9m7b
Deposition date deposition_date2025-03-10
Structure title titleStructure of flagellar hook at 3.14 angstroms resolution,conformation 2.
Keywords keywordsflagellum, hook, FlgE, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron103.60
Forward intensity I(0) i0116224000000.00
Molecular weight molecular_weight2776700.0 kDa
Excluded volume excluded_volume3417000 ų
Envelope volume envelope_volume5662000 ų
Hydration-shell volume shell_volume436370 ų
Envelope diameter envelope_diameter413.5
Shell Rg shell_rg108.60
Envelope Rg envelope_rg104.30
Shape Rg shape_rg103.60
Total Rg total_rg103.60
Total atoms total_atoms195294
Residues n_residues26532
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 dmax295.4
Rg (real space) rg_real98.62
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real1.1130e+11
I(0) uncertainty (real space) i0_real_error2.3300e+09
Rg (reciprocal space) rg_reciprocal100.20
I(0) (reciprocal space) i0_reciprocal115100000000.0000
Solution quality estimate total_estimate0.8981
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary118.2
Skewness Skewness skewness0.430
Kurtosis Kurtosis kurtosis-0.270
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.7223
Highest regularization parameter α highest_alpha37680000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.937; Stabil: 0.975; Sysdev: 1.000; Positv: 1.000; Valcen: 0.925; Smooth: 0.013

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)