9ygu

Flagella filament structure in H. pylori composed of flagellin FlaA

Method: ELECTRON MICROSCOPY Dmax: 215.7 Å Quality: EXCELLENT

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

Flagellin

OrganismNot specified

UniProt B8Q9B9

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 × 33 PDB declaration: 33-meric(33) Consistent with protein copy count Chain A7; UniProt 2–509 Chain BJ; UniProt 2–509 Chain CT; UniProt 2–509 Chain DN; UniProt 2–509 Chain EX; UniProt 2–509 Chain FB; UniProt 2–509 Chain GQ; UniProt 2–509 Chain HL; UniProt 2–509 Chain I3; UniProt 2–509 Chain JD; UniProt 2–509 Chain KE; UniProt 2–509 Chain LF; UniProt 2–509 Chain MO; UniProt 2–509 Chain NI; UniProt 2–509 Chain OA; UniProt 2–509 Chain PU; UniProt 2–509 Chain Q2; UniProt 2–509 Chain R4; UniProt 2–509 Chain S5; UniProt 2–509 Chain TP; UniProt 2–509 Chain UH; UniProt 2–509 Chain VR; UniProt 2–509 Chain WG; UniProt 2–509 Chain XM; UniProt 2–509 Chain Y1; UniProt 2–509 Chain Z9; UniProt 2–509 Chain aW; UniProt 2–509 Chain bS; UniProt 2–509 Chain cV; UniProt 2–509 Chain dC; UniProt 2–509 Chain e8; UniProt 2–509 Chain fK; UniProt 2–509 Chain g6; UniProt 2–509 Not recorded P8E 5,7-diamino-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno-non-2-ulopyranosonic acid × 231 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.88 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name B8Q9B9_HELPX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A7; PDBConstruct 1–508; UniProt 2–509 Author chain BJ; PDBConstruct 1–508; UniProt 2–509 Author chain CT; PDBConstruct 1–508; UniProt 2–509 Author chain DN; PDBConstruct 1–508; UniProt 2–509 Author chain EX; PDBConstruct 1–508; UniProt 2–509 Author chain FB; PDBConstruct 1–508; UniProt 2–509 Author chain GQ; PDBConstruct 1–508; UniProt 2–509 Author chain HL; PDBConstruct 1–508; UniProt 2–509 Author chain I3; PDBConstruct 1–508; UniProt 2–509 Author chain JD; PDBConstruct 1–508; UniProt 2–509 Author chain KE; PDBConstruct 1–508; UniProt 2–509 Author chain LF; PDBConstruct 1–508; UniProt 2–509 Author chain MO; PDBConstruct 1–508; UniProt 2–509 Author chain NI; PDBConstruct 1–508; UniProt 2–509 Author chain OA; PDBConstruct 1–508; UniProt 2–509 Author chain PU; PDBConstruct 1–508; UniProt 2–509 Author chain Q2; PDBConstruct 1–508; UniProt 2–509 Author chain R4; PDBConstruct 1–508; UniProt 2–509 Author chain S5; PDBConstruct 1–508; UniProt 2–509 Author chain TP; PDBConstruct 1–508; UniProt 2–509 Author chain UH; PDBConstruct 1–508; UniProt 2–509 Author chain VR; PDBConstruct 1–508; UniProt 2–509 Author chain WG; PDBConstruct 1–508; UniProt 2–509 Author chain XM; PDBConstruct 1–508; UniProt 2–509 Author chain Y1; PDBConstruct 1–508; UniProt 2–509 Author chain Z9; PDBConstruct 1–508; UniProt 2–509 Author chain aW; PDBConstruct 1–508; UniProt 2–509 Author chain bS; PDBConstruct 1–508; UniProt 2–509 Author chain cV; PDBConstruct 1–508; UniProt 2–509 Author chain dC; PDBConstruct 1–508; UniProt 2–509 Author chain e8; PDBConstruct 1–508; UniProt 2–509 Author chain fK; PDBConstruct 1–508; UniProt 2–509 Author chain g6; PDBConstruct 1–508; UniProt 2–509

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 9ygu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ygu
Deposition date deposition_date2025-09-29
Structure title titleFlagella filament structure in H. pylori composed of flagellin FlaA
Keywords keywordsflagellin, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier82.91
Radius of gyration Rg (electron density) rg_electron82.61
Forward intensity I(0) i049601200000.00
Molecular weight molecular_weight1803000.0 kDa
Excluded volume excluded_volume2223400 ų
Envelope volume envelope_volume3191700 ų
Hydration-shell volume shell_volume304370 ų
Envelope diameter envelope_diameter330.4
Shell Rg shell_rg93.67
Envelope Rg envelope_rg81.94
Shape Rg shape_rg82.61
Total Rg total_rg82.68
Total atoms total_atoms129921
Residues n_residues16764
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 dmax215.7
Rg (real space) rg_real79.06
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real4.7420e+10
I(0) uncertainty (real space) i0_real_error7.0760e+08
Rg (reciprocal space) rg_reciprocal83.46
I(0) (reciprocal space) i0_reciprocal49680000000.0000
Solution quality estimate total_estimate0.9111
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary102.2
Skewness Skewness skewness0.107
Kurtosis Kurtosis kurtosis-0.435
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.3996
Highest regularization parameter α highest_alpha10690000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.980; Stabil: 0.989; Sysdev: 1.000; Positv: 1.000; Valcen: 0.934; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)