8uox

Cryo-EM structure of a Counterclockwise locked form of the Salmonella enterica Typhimurium flagellar C-ring, with C34 symmetry applied

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Flagellar M-ring protein

OrganismNot specified

UniProt P15928

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 204 Flagellar motor switch protein FliG × 34 (P0A1J9) Flagellar motor switch protein FliM × 34 (P26418) Flagellar motor switch protein FliN × 102 (P26419) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FLIF_SALTY
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A1; PDBConstruct 1–560; UniProt 1–560 Author chain A2; PDBConstruct 1–560; UniProt 1–560 Author chain A3; PDBConstruct 1–560; UniProt 1–560 Author chain A4; PDBConstruct 1–560; UniProt 1–560 Author chain A5; PDBConstruct 1–560; UniProt 1–560 Author chain A6; PDBConstruct 1–560; UniProt 1–560 Author chain A7; PDBConstruct 1–560; UniProt 1–560 Author chain A8; PDBConstruct 1–560; UniProt 1–560 Author chain A9; PDBConstruct 1–560; UniProt 1–560 Author chain AA; PDBConstruct 1–560; UniProt 1–560 Author chain AB; PDBConstruct 1–560; UniProt 1–560 Author chain AC; PDBConstruct 1–560; UniProt 1–560 Author chain AD; PDBConstruct 1–560; UniProt 1–560 Author chain AE; PDBConstruct 1–560; UniProt 1–560 Author chain AF; PDBConstruct 1–560; UniProt 1–560 Author chain AG; PDBConstruct 1–560; UniProt 1–560 Author chain AH; PDBConstruct 1–560; UniProt 1–560 Author chain AI; PDBConstruct 1–560; UniProt 1–560 Author chain AJ; PDBConstruct 1–560; UniProt 1–560 Author chain AK; PDBConstruct 1–560; UniProt 1–560 Author chain AL; PDBConstruct 1–560; UniProt 1–560 Author chain AM; PDBConstruct 1–560; UniProt 1–560 Author chain AN; PDBConstruct 1–560; UniProt 1–560 Author chain AO; PDBConstruct 1–560; UniProt 1–560 Author chain AP; PDBConstruct 1–560; UniProt 1–560 Author chain AQ; PDBConstruct 1–560; UniProt 1–560 Author chain AR; PDBConstruct 1–560; UniProt 1–560 Author chain AS; PDBConstruct 1–560; UniProt 1–560 Author chain AT; PDBConstruct 1–560; UniProt 1–560 Author chain AU; PDBConstruct 1–560; UniProt 1–560 Author chain AV; PDBConstruct 1–560; UniProt 1–560 Author chain AW; PDBConstruct 1–560; UniProt 1–560 Author chain AX; PDBConstruct 1–560; UniProt 1–560 Author chain AY; PDBConstruct 1–560; UniProt 1–560

Flagellar motor switch protein FliG

OrganismNot specified

UniProt P0A1J9

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 204 Flagellar M-ring protein × 34 (P15928) Flagellar motor switch protein FliM × 34 (P26418) Flagellar motor switch protein FliN × 102 (P26419) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FLIG_SALTY
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B1; PDBConstruct 1–331; UniProt 1–331 Author chain B2; PDBConstruct 1–331; UniProt 1–331 Author chain B3; PDBConstruct 1–331; UniProt 1–331 Author chain B4; PDBConstruct 1–331; UniProt 1–331 Author chain B5; PDBConstruct 1–331; UniProt 1–331 Author chain B6; PDBConstruct 1–331; UniProt 1–331 Author chain B7; PDBConstruct 1–331; UniProt 1–331 Author chain B8; PDBConstruct 1–331; UniProt 1–331 Author chain B9; PDBConstruct 1–331; UniProt 1–331 Author chain BA; PDBConstruct 1–331; UniProt 1–331 Author chain BB; PDBConstruct 1–331; UniProt 1–331 Author chain BC; PDBConstruct 1–331; UniProt 1–331 Author chain BD; PDBConstruct 1–331; UniProt 1–331 Author chain BE; PDBConstruct 1–331; UniProt 1–331 Author chain BF; PDBConstruct 1–331; UniProt 1–331 Author chain BG; PDBConstruct 1–331; UniProt 1–331 Author chain BH; PDBConstruct 1–331; UniProt 1–331 Author chain BI; PDBConstruct 1–331; UniProt 1–331 Author chain BJ; PDBConstruct 1–331; UniProt 1–331 Author chain BK; PDBConstruct 1–331; UniProt 1–331 Author chain BL; PDBConstruct 1–331; UniProt 1–331 Author chain BM; PDBConstruct 1–331; UniProt 1–331 Author chain BN; PDBConstruct 1–331; UniProt 1–331 Author chain BO; PDBConstruct 1–331; UniProt 1–331 Author chain BP; PDBConstruct 1–331; UniProt 1–331 Author chain BQ; PDBConstruct 1–331; UniProt 1–331 Author chain BR; PDBConstruct 1–331; UniProt 1–331 Author chain BS; PDBConstruct 1–331; UniProt 1–331 Author chain BT; PDBConstruct 1–331; UniProt 1–331 Author chain BU; PDBConstruct 1–331; UniProt 1–331 Author chain BV; PDBConstruct 1–331; UniProt 1–331 Author chain BW; PDBConstruct 1–331; UniProt 1–331 Author chain BX; PDBConstruct 1–331; UniProt 1–331 Author chain BY; PDBConstruct 1–331; UniProt 1–331

Flagellar motor switch protein FliM

OrganismNot specified

UniProt P26418

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 204 Flagellar M-ring protein × 34 (P15928) Flagellar motor switch protein FliG × 34 (P0A1J9) Flagellar motor switch protein FliN × 102 (P26419) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FLIM_SALTY
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C1; PDBConstruct 1–334; UniProt 1–334 Author chain C2; PDBConstruct 1–334; UniProt 1–334 Author chain C3; PDBConstruct 1–334; UniProt 1–334 Author chain C4; PDBConstruct 1–334; UniProt 1–334 Author chain C5; PDBConstruct 1–334; UniProt 1–334 Author chain C6; PDBConstruct 1–334; UniProt 1–334 Author chain C7; PDBConstruct 1–334; UniProt 1–334 Author chain C8; PDBConstruct 1–334; UniProt 1–334 Author chain C9; PDBConstruct 1–334; UniProt 1–334 Author chain CA; PDBConstruct 1–334; UniProt 1–334 Author chain CB; PDBConstruct 1–334; UniProt 1–334 Author chain CC; PDBConstruct 1–334; UniProt 1–334 Author chain CD; PDBConstruct 1–334; UniProt 1–334 Author chain CE; PDBConstruct 1–334; UniProt 1–334 Author chain CF; PDBConstruct 1–334; UniProt 1–334 Author chain CG; PDBConstruct 1–334; UniProt 1–334 Author chain CH; PDBConstruct 1–334; UniProt 1–334 Author chain CI; PDBConstruct 1–334; UniProt 1–334 Author chain CJ; PDBConstruct 1–334; UniProt 1–334 Author chain CK; PDBConstruct 1–334; UniProt 1–334 Author chain CL; PDBConstruct 1–334; UniProt 1–334 Author chain CM; PDBConstruct 1–334; UniProt 1–334 Author chain CN; PDBConstruct 1–334; UniProt 1–334 Author chain CO; PDBConstruct 1–334; UniProt 1–334 Author chain CP; PDBConstruct 1–334; UniProt 1–334 Author chain CQ; PDBConstruct 1–334; UniProt 1–334 Author chain CR; PDBConstruct 1–334; UniProt 1–334 Author chain CS; PDBConstruct 1–334; UniProt 1–334 Author chain CT; PDBConstruct 1–334; UniProt 1–334 Author chain CU; PDBConstruct 1–334; UniProt 1–334 Author chain CV; PDBConstruct 1–334; UniProt 1–334 Author chain CW; PDBConstruct 1–334; UniProt 1–334 Author chain CX; PDBConstruct 1–334; UniProt 1–334 Author chain CY; PDBConstruct 1–334; UniProt 1–334

Flagellar motor switch protein FliN

OrganismNot specified

UniProt P26419

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 204 Flagellar M-ring protein × 34 (P15928) Flagellar motor switch protein FliG × 34 (P0A1J9) Flagellar motor switch protein FliM × 34 (P26418) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FLIN_SALTY
Isoform —
PDB entities 4
Chains and sequence ranges Author chain D1; PDBConstruct 1–137; UniProt 1–137 Author chain D2; PDBConstruct 1–137; UniProt 1–137 Author chain D3; PDBConstruct 1–137; UniProt 1–137 Author chain D4; PDBConstruct 1–137; UniProt 1–137 Author chain D5; PDBConstruct 1–137; UniProt 1–137 Author chain D6; PDBConstruct 1–137; UniProt 1–137 Author chain D7; PDBConstruct 1–137; UniProt 1–137 Author chain D8; PDBConstruct 1–137; UniProt 1–137 Author chain D9; PDBConstruct 1–137; UniProt 1–137 Author chain DA; PDBConstruct 1–137; UniProt 1–137 Author chain DB; PDBConstruct 1–137; UniProt 1–137 Author chain DC; PDBConstruct 1–137; UniProt 1–137 Author chain DD; PDBConstruct 1–137; UniProt 1–137 Author chain DE; PDBConstruct 1–137; UniProt 1–137 Author chain DF; PDBConstruct 1–137; UniProt 1–137 Author chain DG; PDBConstruct 1–137; UniProt 1–137 Author chain DH; PDBConstruct 1–137; UniProt 1–137 Author chain DI; PDBConstruct 1–137; UniProt 1–137 Author chain DJ; PDBConstruct 1–137; UniProt 1–137 Author chain DK; PDBConstruct 1–137; UniProt 1–137 Author chain DL; PDBConstruct 1–137; UniProt 1–137 Author chain DM; PDBConstruct 1–137; UniProt 1–137 Author chain DN; PDBConstruct 1–137; UniProt 1–137 Author chain DO; PDBConstruct 1–137; UniProt 1–137 Author chain DP; PDBConstruct 1–137; UniProt 1–137 Author chain DQ; PDBConstruct 1–137; UniProt 1–137 Author chain DR; PDBConstruct 1–137; UniProt 1–137 Author chain DS; PDBConstruct 1–137; UniProt 1–137 Author chain DT; PDBConstruct 1–137; UniProt 1–137 Author chain DU; PDBConstruct 1–137; UniProt 1–137 Author chain DV; PDBConstruct 1–137; UniProt 1–137 Author chain DW; PDBConstruct 1–137; UniProt 1–137 Author chain DX; PDBConstruct 1–137; UniProt 1–137 Author chain DY; PDBConstruct 1–137; UniProt 1–137 Author chain E1; PDBConstruct 1–137; UniProt 1–137 Author chain E2; PDBConstruct 1–137; UniProt 1–137 Author chain E3; PDBConstruct 1–137; UniProt 1–137 Author chain E4; PDBConstruct 1–137; UniProt 1–137 Author chain E5; PDBConstruct 1–137; UniProt 1–137 Author chain E6; PDBConstruct 1–137; UniProt 1–137 Author chain E7; PDBConstruct 1–137; UniProt 1–137 Author chain E8; PDBConstruct 1–137; UniProt 1–137 Author chain E9; PDBConstruct 1–137; UniProt 1–137 Author chain EA; PDBConstruct 1–137; UniProt 1–137 Author chain EB; PDBConstruct 1–137; UniProt 1–137 Author chain EC; PDBConstruct 1–137; UniProt 1–137 Author chain ED; PDBConstruct 1–137; UniProt 1–137 Author chain EE; PDBConstruct 1–137; UniProt 1–137 Author chain EF; PDBConstruct 1–137; UniProt 1–137 Author chain EG; PDBConstruct 1–137; UniProt 1–137 Author chain EH; PDBConstruct 1–137; UniProt 1–137 Author chain EI; PDBConstruct 1–137; UniProt 1–137 Author chain EJ; PDBConstruct 1–137; UniProt 1–137 Author chain EK; PDBConstruct 1–137; UniProt 1–137 Author chain EL; PDBConstruct 1–137; UniProt 1–137 Author chain EM; PDBConstruct 1–137; UniProt 1–137 Author chain EN; PDBConstruct 1–137; UniProt 1–137 Author chain EO; PDBConstruct 1–137; UniProt 1–137 Author chain EP; PDBConstruct 1–137; UniProt 1–137 Author chain EQ; PDBConstruct 1–137; UniProt 1–137 Author chain ER; PDBConstruct 1–137; UniProt 1–137 Author chain ES; PDBConstruct 1–137; UniProt 1–137 Author chain ET; PDBConstruct 1–137; UniProt 1–137 Author chain EU; PDBConstruct 1–137; UniProt 1–137 Author chain EV; PDBConstruct 1–137; UniProt 1–137 Author chain EW; PDBConstruct 1–137; UniProt 1–137 Author chain EX; PDBConstruct 1–137; UniProt 1–137 Author chain EY; PDBConstruct 1–137; UniProt 1–137 Author chain F1; PDBConstruct 1–137; UniProt 1–137 Author chain F2; PDBConstruct 1–137; UniProt 1–137 Author chain F3; PDBConstruct 1–137; UniProt 1–137 Author chain F4; PDBConstruct 1–137; UniProt 1–137 Author chain F5; PDBConstruct 1–137; UniProt 1–137 Author chain F6; PDBConstruct 1–137; UniProt 1–137 Author chain F7; PDBConstruct 1–137; UniProt 1–137 Author chain F8; PDBConstruct 1–137; UniProt 1–137 Author chain F9; PDBConstruct 1–137; UniProt 1–137 Author chain FA; PDBConstruct 1–137; UniProt 1–137 Author chain FB; PDBConstruct 1–137; UniProt 1–137 Author chain FC; PDBConstruct 1–137; UniProt 1–137 Author chain FD; PDBConstruct 1–137; UniProt 1–137 Author chain FE; PDBConstruct 1–137; UniProt 1–137 Author chain FF; PDBConstruct 1–137; UniProt 1–137 Author chain FG; PDBConstruct 1–137; UniProt 1–137 Author chain FH; PDBConstruct 1–137; UniProt 1–137 Author chain FI; PDBConstruct 1–137; UniProt 1–137 Author chain FJ; PDBConstruct 1–137; UniProt 1–137 Author chain FK; PDBConstruct 1–137; UniProt 1–137 Author chain FL; PDBConstruct 1–137; UniProt 1–137 Author chain FM; PDBConstruct 1–137; UniProt 1–137 Author chain FN; PDBConstruct 1–137; UniProt 1–137 Author chain FO; PDBConstruct 1–137; UniProt 1–137 Author chain FP; PDBConstruct 1–137; UniProt 1–137 Author chain FQ; PDBConstruct 1–137; UniProt 1–137 Author chain FR; PDBConstruct 1–137; UniProt 1–137 Author chain FS; PDBConstruct 1–137; UniProt 1–137 Author chain FT; PDBConstruct 1–137; UniProt 1–137 Author chain FU; PDBConstruct 1–137; UniProt 1–137 Author chain FV; PDBConstruct 1–137; UniProt 1–137 Author chain FW; PDBConstruct 1–137; UniProt 1–137 Author chain FX; PDBConstruct 1–137; UniProt 1–137 Author chain FY; PDBConstruct 1–137; UniProt 1–137

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id8uox
Deposition date deposition_date2023-10-20
Structure title titleCryo-EM structure of a Counterclockwise locked form of the Salmonella enterica Typhimurium flagellar C-ring, with C34 symmetry applied
Keywords keywordsFlagella, Salmonella, C-ring, motor, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

8uox__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8uox__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 108 109 1010 1011 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8uox__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)0.00 Å
Rg (electron density)206.60 Å
Total Rg206.60 Å
Atom count244834
Residues30974
Excluded volume4385500 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8uox__assembly_1__model_1 204-meric (204) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

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7. Citations (1)