3soh

Architecture of the Flagellar Rotor

Method: X-RAY DIFFRACTION Dmax: 92.6 Å Quality: GOOD

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

Flagellar motor switch protein FliM

Thermotoga maritima

UniProt Q9WZE6

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 46–233 Fragment:N-terminal domain (UNP residues 46-233) Flagellar motor switch protein FliG × 1 (Q9WY63) X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.5;0.1 M MES, pH 6.5, 10% dioxane, 1.6 M ammonium sulfate, EVAPORATION Resolution 3.50 Å R-free 0.301
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 46–233 Fragment:N-terminal domain (UNP residues 46-233) Flagellar motor switch protein FliG × 1 (Q9WY63) X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.5;0.1 M MES, pH 6.5, 10% dioxane, 1.6 M ammonium sulfate, EVAPORATION Resolution 3.50 Å R-free 0.301

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.

4 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9WZE6_THEMA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–188; UniProt 46–233 Author chain C; PDBConstruct 1–188; UniProt 46–233

Flagellar motor switch protein FliG

Thermotoga maritima

UniProt Q9WY63

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 117–193 Fragment:middle domain (UNP residues 117-193) Flagellar motor switch protein FliM × 1 (Q9WZE6) X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.5;0.1 M MES, pH 6.5, 10% dioxane, 1.6 M ammonium sulfate, EVAPORATION Resolution 3.50 Å R-free 0.301
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 117–193 Fragment:middle domain (UNP residues 117-193) Flagellar motor switch protein FliM × 1 (Q9WZE6) X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.5;0.1 M MES, pH 6.5, 10% dioxane, 1.6 M ammonium sulfate, EVAPORATION Resolution 3.50 Å R-free 0.301

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.

6 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIG_THEMA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–80; UniProt 117–193 Author chain D; PDBConstruct 5–80; UniProt 117–193

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 3soh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3soh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3soh
Deposition date deposition_date2011-06-30
Structure title titleArchitecture of the Flagellar Rotor
Keywords keywordsprotein-protein complex, alpha/beta, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.01
Radius of gyration Rg (electron density) rg_electron26.09
Forward intensity I(0) i054541500.00
Molecular weight molecular_weight60702.0 kDa
Excluded volume excluded_volume77235 ų
Envelope volume envelope_volume95580 ų
Hydration-shell volume shell_volume30724 ų
Envelope diameter envelope_diameter93.7
Shell Rg shell_rg33.22
Envelope Rg envelope_rg26.27
Shape Rg shape_rg26.08
Total Rg total_rg26.92
Total atoms total_atoms4284
Residues n_residues536
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 dmax92.6
Rg (real space) rg_real27.02
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real5.4540e+07
I(0) uncertainty (real space) i0_real_error7.6180e+05
Rg (reciprocal space) rg_reciprocal27.02
I(0) (reciprocal space) i0_reciprocal54540000.0000
Solution quality estimate total_estimate0.8663
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.8
Skewness Skewness skewness0.386
Kurtosis Kurtosis kurtosis-0.196
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38800000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.801; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.912

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3sohA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1550 — Chemotaxis protein chec
Homologous superfamily homologous superfamily10 — CheC-like
Domain ID domain_id3sohB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily30 — Flagellar motor switch protein FliG, alpha-alpha superhelical domain
Domain ID domain_id3sohC00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1550 — Chemotaxis protein chec
Homologous superfamily homologous superfamily10 — CheC-like
Domain ID domain_id3sohD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily30 — Flagellar motor switch protein FliG, alpha-alpha superhelical domain

8. Citations (1)

9. Files and Curves (10)