9YDT image
Deposition Date 2025-09-23
Release Date 2026-06-10
Last Version Date 2026-06-10
Entry Detail
PDB ID:
9YDT
Keywords:
Title:
LPHT-ring in Vibrio cholerae at disassembled, closed state
Biological Source:
Method Details:
Experimental Method:
Resolution:
2.75 Å
Aggregation State:
CELL
Reconstruction Method:
SINGLE PARTICLE
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Flagellar L-ring protein
Gene (Uniprot):flgH
Chain IDs:A (auth: Aa), B (auth: Ab), C (auth: Ac), D (auth: Ad), E (auth: Ae), F (auth: Af), G (auth: Ag), H (auth: Ah), I (auth: Ai), J (auth: Aj), K (auth: Ak), L (auth: Al), M (auth: Am), N (auth: An), O (auth: Ao), P (auth: Ap), Q (auth: Aq), R (auth: Ar), S (auth: As), T (auth: At), U (auth: Au), V (auth: Av), W (auth: Aw), X (auth: Ax), Y (auth: Ay), Z (auth: Az)
Chain Length:227
Number of Molecules:26
Biological Source:Vibrio cholerae O1 biovar El Tor str. N16961
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Flagellar P-ring protein
Gene (Uniprot):flgI
Chain IDs:AA (auth: Ba), BA (auth: Bb), CA (auth: Bc), DA (auth: Bd), EA (auth: Be), FA (auth: Bf), GA (auth: Bg), HA (auth: Bh), IA (auth: Bi), JA (auth: Bj), KA (auth: Bk), LA (auth: Bl), MA (auth: Bm), NA (auth: Bn), OA (auth: Bo), PA (auth: Bp), QA (auth: Bq), RA (auth: Br), SA (auth: Bs), TA (auth: Bt), UA (auth: Bu), VA (auth: Bv), WA (auth: Bw), XA (auth: Bx), YA (auth: By), ZA (auth: Bz)
Chain Length:343
Number of Molecules:26
Biological Source:Vibrio cholerae O1 biovar El Tor str. N16961
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Flagellar protein FlgT
Gene (Uniprot):VC_2208
Chain IDs:AB (auth: Ca), BB (auth: Cb), CB (auth: Cc), DB (auth: Cd), EB (auth: Ce), FB (auth: Cf), GB (auth: Cg), HB (auth: Ch), IB (auth: Ci), JB (auth: Cj), KB (auth: Ck), LB (auth: Cl), MB (auth: Cm), NB (auth: Cn), OB (auth: Co), PB (auth: Cp), QB (auth: Cq), RB (auth: Cr), SB (auth: Cs), TB (auth: Ct), UB (auth: Cu), VB (auth: Cv), WB (auth: Cw), XB (auth: Cx), YB (auth: Cy), ZB (auth: Cz)
Chain Length:352
Number of Molecules:26
Biological Source:Vibrio cholerae O1 biovar El Tor str. N16961
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Sodium-type flagellar protein
Gene (Uniprot):VC_1008
Chain IDs:AC (auth: Da), BC (auth: Db), CC (auth: Dc), DC (auth: Dd), EC (auth: De), FC (auth: Df), GC (auth: Dg), HC (auth: Dh), IC (auth: Di), JC (auth: Dj), KC (auth: Dk), LC (auth: Dl), MC (auth: Dm), NC (auth: Dn), OC (auth: Do), PC (auth: Dp), QC (auth: Dq), RC (auth: Dr), SC (auth: Ds), TC (auth: Dt), UC (auth: Du), VC (auth: Dv), WC (auth: Dw), XC (auth: Dx), YC (auth: Dy), ZC (auth: Dz)
Chain Length:272
Number of Molecules:26
Biological Source:Vibrio cholerae O1 biovar El Tor str. N16961
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Flagellar assembly lipoprotei
Gene (Uniprot):flgP
Chain IDs:AD (auth: Fa), BD (auth: Fb), CD (auth: Fc), DD (auth: Fd), ED (auth: Fe), FD (auth: Ff), GD (auth: Fg), HD (auth: Fh), ID (auth: Fi), JD (auth: Fj), KD (auth: Fk), LD (auth: Fl), MD (auth: Fm), ND (auth: Fn), OD (auth: Fo), PD (auth: Fp), QD (auth: Fq), RD (auth: Fr), SD (auth: Fs), TD (auth: Ft), UD (auth: Fu), VD (auth: Fv), WD (auth: Fw), XD (auth: Fx), YD (auth: Fy), ZD (auth: Fz), AE (auth: Ga), BE (auth: Gb), CE (auth: Gc), DE (auth: Gd), EE (auth: Ge), FE (auth: Gf), GE (auth: Gg), HE (auth: Gh), IE (auth: Gi), JE (auth: Gj), KE (auth: Gk), LE (auth: Gl), ME (auth: Gm), NE (auth: Gn), OE (auth: Go), PE (auth: Gp), QE (auth: Gq), RE (auth: Gr), SE (auth: Gs), TE (auth: Gt), UE (auth: Gu), VE (auth: Gv), WE (auth: Gw), XE (auth: Gx), YE (auth: Gy), ZE (auth: Gz)
Chain Length:15
Number of Molecules:52
Biological Source:Vibrio cholerae O1 biovar El Tor str. N16961
Ligand Molecules
Primary Citation
In-situ cryo-EM structures reveal mechanisms of sheathed flagellar assembly, rotation, and disassembly in Vibrio cholerae
To Be Published ? ? ? (?)
Primary Citation of related structures
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