Flagellar motor switch protein FliM
Thermotoga maritima
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 46–228 | Fragment:Middle domain, Chain A, C, E, G, I, K, M, O, Q, S, U | Flagellar motor switch protein FliG × 1 (Q9WY63) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M imidazole, pH 6.5, 1.2 M sodium acetate trihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 4.32 Å R-free 0.291 |
| 10 | Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain M; UniProt 46–228 | Fragment:Middle domain, Chain A, C, E, G, I, K, M, O, Q, S, U | Flagellar motor switch protein FliG × 1 (Q9WY63) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M imidazole, pH 6.5, 1.2 M sodium acetate trihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 4.32 Å R-free 0.291 |
| 11 | Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain O; UniProt 46–228 | Fragment:Middle domain, Chain A, C, E, G, I, K, M, O, Q, S, U | Flagellar motor switch protein FliG × 1 (Q9WY63) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M imidazole, pH 6.5, 1.2 M sodium acetate trihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 4.32 Å R-free 0.291 |
| 2 | Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain C; UniProt 46–228 | Fragment:Middle domain, Chain A, C, E, G, I, K, M, O, Q, S, U | Flagellar motor switch protein FliG × 1 (Q9WY63) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M imidazole, pH 6.5, 1.2 M sodium acetate trihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 4.32 Å R-free 0.291 |
| 3 | Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain E; UniProt 46–228 | Fragment:Middle domain, Chain A, C, E, G, I, K, M, O, Q, S, U | Flagellar motor switch protein FliG × 1 (Q9WY63) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M imidazole, pH 6.5, 1.2 M sodium acetate trihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 4.32 Å R-free 0.291 |
| 4 | Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain G; UniProt 46–228 | Fragment:Middle domain, Chain A, C, E, G, I, K, M, O, Q, S, U | Flagellar motor switch protein FliG × 1 (Q9WY63) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M imidazole, pH 6.5, 1.2 M sodium acetate trihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 4.32 Å R-free 0.291 |
| 5 | Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain I; UniProt 46–228 | Fragment:Middle domain, Chain A, C, E, G, I, K, M, O, Q, S, U | Flagellar motor switch protein FliG × 1 (Q9WY63) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M imidazole, pH 6.5, 1.2 M sodium acetate trihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 4.32 Å R-free 0.291 |
| 6 | Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain Q; UniProt 46–228 | Fragment:Middle domain, Chain A, C, E, G, I, K, M, O, Q, S, U | Flagellar motor switch protein FliG × 1 (Q9WY63) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M imidazole, pH 6.5, 1.2 M sodium acetate trihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 4.32 Å R-free 0.291 |
| 7 | Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain S; UniProt 46–228 | Fragment:Middle domain, Chain A, C, E, G, I, K, M, O, Q, S, U | Flagellar motor switch protein FliG × 1 (Q9WY63) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M imidazole, pH 6.5, 1.2 M sodium acetate trihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 4.32 Å R-free 0.291 |
| 8 | Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain U; UniProt 46–228 | Fragment:Middle domain, Chain A, C, E, G, I, K, M, O, Q, S, U | Flagellar motor switch protein FliG × 1 (Q9WY63) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M imidazole, pH 6.5, 1.2 M sodium acetate trihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 4.32 Å R-free 0.291 |
| 9 | Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain K; UniProt 46–228 | Fragment:Middle domain, Chain A, C, E, G, I, K, M, O, Q, S, U | Flagellar motor switch protein FliG × 1 (Q9WY63) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M imidazole, pH 6.5, 1.2 M sodium acetate trihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K | Resolution 4.32 Å R-free 0.291 |
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 5 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | FLIM_THEMA |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 1–183; UniProt 46–228 Author chain C; PDBConstruct 1–183; UniProt 46–228 Author chain E; PDBConstruct 1–183; UniProt 46–228 Author chain G; PDBConstruct 1–183; UniProt 46–228 Author chain I; PDBConstruct 1–183; UniProt 46–228 Author chain K; PDBConstruct 1–183; UniProt 46–228 Author chain M; PDBConstruct 1–183; UniProt 46–228 Author chain O; PDBConstruct 1–183; UniProt 46–228 Author chain Q; PDBConstruct 1–183; UniProt 46–228 Author chain S; PDBConstruct 1–183; UniProt 46–228 Author chain U; PDBConstruct 1–183; UniProt 46–228 |