9iyc

P ring on polyrod-P ring complex from Salmonella TH26292 strain

Method: ELECTRON MICROSCOPY Dmax: 248.7 Å Quality: REASONABLE

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

Flagellar P-ring protein

Salmonella enterica subsp. enterica serovar Typhimurium

UniProt P15930

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 × 26 PDB declaration: 26-meric(26) Consistent with protein copy count Chain A; UniProt 20–365 Chain B; UniProt 20–365 Chain C; UniProt 20–365 Chain D; UniProt 20–365 Chain E; UniProt 20–365 Chain F; UniProt 20–365 Chain G; UniProt 20–365 Chain H; UniProt 20–365 Chain I; UniProt 20–365 Chain J; UniProt 20–365 Chain K; UniProt 20–365 Chain L; UniProt 20–365 Chain M; UniProt 20–365 Chain N; UniProt 20–365 Chain O; UniProt 20–365 Chain P; UniProt 20–365 Chain Q; UniProt 20–365 Chain R; UniProt 20–365 Chain S; UniProt 20–365 Chain T; UniProt 20–365 Chain U; UniProt 20–365 Chain V; UniProt 20–365 Chain W; UniProt 20–365 Chain X; UniProt 20–365 Chain Y; UniProt 20–365 Chain Z; UniProt 20–365 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;BLOTTING TIME OF 4 SECONDS, 1 SECONDS DRAIN TIME, FORCE 0 Resolution 2.33 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGI_SALTY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–346; UniProt 20–365 Author chain B; PDBConstruct 1–346; UniProt 20–365 Author chain C; PDBConstruct 1–346; UniProt 20–365 Author chain D; PDBConstruct 1–346; UniProt 20–365 Author chain E; PDBConstruct 1–346; UniProt 20–365 Author chain F; PDBConstruct 1–346; UniProt 20–365 Author chain G; PDBConstruct 1–346; UniProt 20–365 Author chain H; PDBConstruct 1–346; UniProt 20–365 Author chain I; PDBConstruct 1–346; UniProt 20–365 Author chain J; PDBConstruct 1–346; UniProt 20–365 Author chain K; PDBConstruct 1–346; UniProt 20–365 Author chain L; PDBConstruct 1–346; UniProt 20–365 Author chain M; PDBConstruct 1–346; UniProt 20–365 Author chain N; PDBConstruct 1–346; UniProt 20–365 Author chain O; PDBConstruct 1–346; UniProt 20–365 Author chain P; PDBConstruct 1–346; UniProt 20–365 Author chain Q; PDBConstruct 1–346; UniProt 20–365 Author chain R; PDBConstruct 1–346; UniProt 20–365 Author chain S; PDBConstruct 1–346; UniProt 20–365 Author chain T; PDBConstruct 1–346; UniProt 20–365 Author chain U; PDBConstruct 1–346; UniProt 20–365 Author chain V; PDBConstruct 1–346; UniProt 20–365 Author chain W; PDBConstruct 1–346; UniProt 20–365 Author chain X; PDBConstruct 1–346; UniProt 20–365 Author chain Y; PDBConstruct 1–346; UniProt 20–365 Author chain Z; PDBConstruct 1–346; UniProt 20–365

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 9iyc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9iyc
Deposition date deposition_date2024-07-30
Structure title titleP ring on polyrod-P ring complex from Salmonella TH26292 strain
Keywords keywordsflagella motor. P ring on polyrod(PaPR) complex, Cryo-EM, SPA, Salmonella, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier95.60
Radius of gyration Rg (electron density) rg_electron94.69
Forward intensity I(0) i010242700000.00
Molecular weight molecular_weight829330.0 kDa
Excluded volume excluded_volume1026900 ų
Envelope volume envelope_volume1921800 ų
Hydration-shell volume shell_volume165360 ų
Envelope diameter envelope_diameter258.8
Shell Rg shell_rg106.90
Envelope Rg envelope_rg85.53
Shape Rg shape_rg94.77
Total Rg total_rg94.49
Total atoms total_atoms57928
Residues n_residues7878
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 dmax248.7
Rg (real space) rg_real95.00
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real1.0230e+10
I(0) uncertainty (real space) i0_real_error2.3270e+08
Rg (reciprocal space) rg_reciprocal96.13
I(0) (reciprocal space) i0_reciprocal10260000000.0000
Solution quality estimate total_estimate0.5734
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary155.4
Skewness Skewness skewness-0.211
Kurtosis Kurtosis kurtosis-1.042
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha0.0340
Highest regularization parameter α highest_alpha117900000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 0.997; Sysdev: 0.000; Positv: 1.000; Valcen: 0.836; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)