Research workbench

CCW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming 34-mer C-ring from Salmonella

Analyse CCW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming 34-mer C-ring… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8T8O
Type: protein
Length: 30,940 residues
Chains: 204
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 4.0
Source: Salmonella enterica subsp. enterica serovar Typhimurium
Molecule: Flagellar M-ring protein; Flagellar motor switch protein FliG; FliM,Flagellar motor…
UniProt: P15928, A0A0F7J9E2, A0A0D6FLG5, A0A0D6FLI0
Pockets: 20 · best druggability 0.81

Structure

electron microscopy · resolution 4.0 · 6 distinct chains · 48% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
F, A, I, S, Z, FA, LA, RA, XA, DB, JB, PB, VB, BC, HC, NC, TC, ZC, FD, LD, RD, XD, DE, JE, PE, VE, BF, HF, NF, TF, ZF, FG, LG, RG	Flagellar M-ring protein	protein	47	89% helix, 0% strand	P15928
G, B, J, T, AA, GA, MA, SA, YA, EB, KB, QB, WB, CC, IC, OC, UC, AD, GD, MD, SD, YD, EE, KE, QE, WE, CF, IF, OF, UF, AG, GG, MG, SG	Flagellar motor switch protein FliG	protein	320	74% helix, 1% strand	A0A0F7J9E2
M, C, K, V, BA, HA, NA, TA, ZA, FB, LB, RB, XB, DC, JC, PC, VC, BD, HD, ND, TD, ZD, FE, LE, RE, XE, DF, JF, PF, VF, BG, HG, NG, TG	FliM,Flagellar motor switch protein FliM	protein	296	33% helix, 27% strand	A0A0D6FLG5
N, D, L, W, CA, IA, OA, UA, AB, GB, MB, SB, YB, EC, KC, QC, WC, CD, ID, OD, UD, AE, GE, ME, SE, YE, EF, KF, QF, WF, CG, IG, OG, UG	Flagellar motor switch protein FliN	protein	93	30% helix, 39% strand	A0A0D6FLI0
P, E, O, X, DA, JA, PA, VA, BB, HB, NB, TB, ZB, FC, LC, RC, XC, DD, JD, PD, VD, BE, HE, NE, TE, ZE, FF, LF, RF, XF, DG, JG, PG, VG	Flagellar motor switch protein FliN	protein	79	19% helix, 23% strand	A0A0D6FLI0
Q, H, R, Y, EA, KA, QA, WA, CB, IB, OB, UB, AC, GC, MC, SC, YC, ED, KD, QD, WD, CE, IE, OE, UE, AF, GF, MF, SF, YF, EG, KG, QG, WG	Flagellar motor switch protein FliN	protein	75	25% helix, 32% strand	A0A0D6FLI0

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1141	0.81	0.82	130	empty
2	982	0.80	0.82	131	empty
3	998	0.80	0.82	136	empty
4	1891	0.80	0.82	227	empty
5	1061	0.80	0.82	157	empty

Interfaces

576 interfaces between chains.

G–SG · 1798 Å² buried · 19 hydrogen bonds · protein-protein
GA–MA · 1793 Å² buried · 18 hydrogen bonds · protein-protein
B–J · 1791 Å² buried · 12 hydrogen bonds · protein-protein
WE–CF · 1784 Å² buried · 17 hydrogen bonds · protein-protein
OC–UC · 1780 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

P15928 · AlphaFold monomer V2.0 prediction for flagellar M-ring protein (P15928) · a predicted model of the same protein · chain FD against A, TM-score 0.63

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P15928
Every structure of UniProt A0A0F7J9E2
Every structure of UniProt A0A0D6FLG5
Every structure of UniProt A0A0D6FLI0
Elsewhere: RCSB PDB 8T8O · PDBe 8T8O · UniProt P15928 · UniProt A0A0F7J9E2 · UniProt A0A0D6FLG5 · UniProt A0A0D6FLI0

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