9yfg

Flagellar outer membrane complex in Vibrio cholerae at disassembled, closed state

Method: ELECTRON MICROSCOPY Dmax: 491.3 Å Quality: GOOD

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

Flagellar L-ring protein

Vibrio cholerae O1 biovar El Tor str. N16961

UniProt Q9KQ13

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 × 298 PDB declaration: 298-meric(298) Consistent with protein copy count Chain Aa; UniProt 32–258 Chain Ab; UniProt 32–258 Chain Ac; UniProt 32–258 Chain Ad; UniProt 32–258 Chain Ae; UniProt 32–258 Chain Af; UniProt 32–258 Chain Ag; UniProt 32–258 Chain Ah; UniProt 32–258 Chain Ai; UniProt 32–258 Chain Aj; UniProt 32–258 Chain Ak; UniProt 32–258 Chain Al; UniProt 32–258 Chain Am; UniProt 32–258 Chain An; UniProt 32–258 Chain Ao; UniProt 32–258 Chain Ap; UniProt 32–258 Chain Aq; UniProt 32–258 Chain Ar; UniProt 32–258 Chain As; UniProt 32–258 Chain At; UniProt 32–258 Chain Au; UniProt 32–258 Chain Av; UniProt 32–258 Chain Aw; UniProt 32–258 Chain Ax; UniProt 32–258 Chain Ay; UniProt 32–258 Chain Az; UniProt 32–258 Not recorded Flagellar P-ring protein × 26 (Q9KQ14) Flagellar protein FlgT × 26 (Q9KPZ9) Sodium-type flagellar protein MotY × 26 (Q9KT95) Sodium-type flagellar protein MotX × 26 (Q9KNX9) FlgP × 52 Lipoprotein × 58 (Q9KQ01) FlgO domain-containing protein × 58 (Q9KQ00) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.55 Å

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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGH_VIBCH
Isoform
PDB entities 1
Chains and sequence ranges Author chain Aa; PDBConstruct 1–227; UniProt 32–258 Author chain Ab; PDBConstruct 1–227; UniProt 32–258 Author chain Ac; PDBConstruct 1–227; UniProt 32–258 Author chain Ad; PDBConstruct 1–227; UniProt 32–258 Author chain Ae; PDBConstruct 1–227; UniProt 32–258 Author chain Af; PDBConstruct 1–227; UniProt 32–258 Author chain Ag; PDBConstruct 1–227; UniProt 32–258 Author chain Ah; PDBConstruct 1–227; UniProt 32–258 Author chain Ai; PDBConstruct 1–227; UniProt 32–258 Author chain Aj; PDBConstruct 1–227; UniProt 32–258 Author chain Ak; PDBConstruct 1–227; UniProt 32–258 Author chain Al; PDBConstruct 1–227; UniProt 32–258 Author chain Am; PDBConstruct 1–227; UniProt 32–258 Author chain An; PDBConstruct 1–227; UniProt 32–258 Author chain Ao; PDBConstruct 1–227; UniProt 32–258 Author chain Ap; PDBConstruct 1–227; UniProt 32–258 Author chain Aq; PDBConstruct 1–227; UniProt 32–258 Author chain Ar; PDBConstruct 1–227; UniProt 32–258 Author chain As; PDBConstruct 1–227; UniProt 32–258 Author chain At; PDBConstruct 1–227; UniProt 32–258 Author chain Au; PDBConstruct 1–227; UniProt 32–258 Author chain Av; PDBConstruct 1–227; UniProt 32–258 Author chain Aw; PDBConstruct 1–227; UniProt 32–258 Author chain Ax; PDBConstruct 1–227; UniProt 32–258 Author chain Ay; PDBConstruct 1–227; UniProt 32–258 Author chain Az; PDBConstruct 1–227; UniProt 32–258

Flagellar P-ring protein

Vibrio cholerae O1 biovar El Tor str. N16961

UniProt Q9KQ14

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 × 298 PDB declaration: 298-meric(298) Consistent with protein copy count Chain Ba; UniProt 19–361 Chain Bb; UniProt 19–361 Chain Bc; UniProt 19–361 Chain Bd; UniProt 19–361 Chain Be; UniProt 19–361 Chain Bf; UniProt 19–361 Chain Bg; UniProt 19–361 Chain Bh; UniProt 19–361 Chain Bi; UniProt 19–361 Chain Bj; UniProt 19–361 Chain Bk; UniProt 19–361 Chain Bl; UniProt 19–361 Chain Bm; UniProt 19–361 Chain Bn; UniProt 19–361 Chain Bo; UniProt 19–361 Chain Bp; UniProt 19–361 Chain Bq; UniProt 19–361 Chain Br; UniProt 19–361 Chain Bs; UniProt 19–361 Chain Bt; UniProt 19–361 Chain Bu; UniProt 19–361 Chain Bv; UniProt 19–361 Chain Bw; UniProt 19–361 Chain Bx; UniProt 19–361 Chain By; UniProt 19–361 Chain Bz; UniProt 19–361 Not recorded Flagellar L-ring protein × 26 (Q9KQ13) Flagellar protein FlgT × 26 (Q9KPZ9) Sodium-type flagellar protein MotY × 26 (Q9KT95) Sodium-type flagellar protein MotX × 26 (Q9KNX9) FlgP × 52 Lipoprotein × 58 (Q9KQ01) FlgO domain-containing protein × 58 (Q9KQ00) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.55 Å

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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGI_VIBCH
Isoform
PDB entities 2
Chains and sequence ranges Author chain Ba; PDBConstruct 1–343; UniProt 19–361 Author chain Bb; PDBConstruct 1–343; UniProt 19–361 Author chain Bc; PDBConstruct 1–343; UniProt 19–361 Author chain Bd; PDBConstruct 1–343; UniProt 19–361 Author chain Be; PDBConstruct 1–343; UniProt 19–361 Author chain Bf; PDBConstruct 1–343; UniProt 19–361 Author chain Bg; PDBConstruct 1–343; UniProt 19–361 Author chain Bh; PDBConstruct 1–343; UniProt 19–361 Author chain Bi; PDBConstruct 1–343; UniProt 19–361 Author chain Bj; PDBConstruct 1–343; UniProt 19–361 Author chain Bk; PDBConstruct 1–343; UniProt 19–361 Author chain Bl; PDBConstruct 1–343; UniProt 19–361 Author chain Bm; PDBConstruct 1–343; UniProt 19–361 Author chain Bn; PDBConstruct 1–343; UniProt 19–361 Author chain Bo; PDBConstruct 1–343; UniProt 19–361 Author chain Bp; PDBConstruct 1–343; UniProt 19–361 Author chain Bq; PDBConstruct 1–343; UniProt 19–361 Author chain Br; PDBConstruct 1–343; UniProt 19–361 Author chain Bs; PDBConstruct 1–343; UniProt 19–361 Author chain Bt; PDBConstruct 1–343; UniProt 19–361 Author chain Bu; PDBConstruct 1–343; UniProt 19–361 Author chain Bv; PDBConstruct 1–343; UniProt 19–361 Author chain Bw; PDBConstruct 1–343; UniProt 19–361 Author chain Bx; PDBConstruct 1–343; UniProt 19–361 Author chain By; PDBConstruct 1–343; UniProt 19–361 Author chain Bz; PDBConstruct 1–343; UniProt 19–361

Flagellar protein FlgT

Vibrio cholerae O1 biovar El Tor str. N16961

UniProt Q9KPZ9

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 × 298 PDB declaration: 298-meric(298) Consistent with protein copy count Chain Ca; UniProt 26–377 Chain Cb; UniProt 26–377 Chain Cc; UniProt 26–377 Chain Cd; UniProt 26–377 Chain Ce; UniProt 26–377 Chain Cf; UniProt 26–377 Chain Cg; UniProt 26–377 Chain Ch; UniProt 26–377 Chain Ci; UniProt 26–377 Chain Cj; UniProt 26–377 Chain Ck; UniProt 26–377 Chain Cl; UniProt 26–377 Chain Cm; UniProt 26–377 Chain Cn; UniProt 26–377 Chain Co; UniProt 26–377 Chain Cp; UniProt 26–377 Chain Cq; UniProt 26–377 Chain Cr; UniProt 26–377 Chain Cs; UniProt 26–377 Chain Ct; UniProt 26–377 Chain Cu; UniProt 26–377 Chain Cv; UniProt 26–377 Chain Cw; UniProt 26–377 Chain Cx; UniProt 26–377 Chain Cy; UniProt 26–377 Chain Cz; UniProt 26–377 Not recorded Flagellar L-ring protein × 26 (Q9KQ13) Flagellar P-ring protein × 26 (Q9KQ14) Sodium-type flagellar protein MotY × 26 (Q9KT95) Sodium-type flagellar protein MotX × 26 (Q9KNX9) FlgP × 52 Lipoprotein × 58 (Q9KQ01) FlgO domain-containing protein × 58 (Q9KQ00) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.55 Å

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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9KPZ9_VIBCH
Isoform
PDB entities 3
Chains and sequence ranges Author chain Ca; PDBConstruct 1–352; UniProt 26–377 Author chain Cb; PDBConstruct 1–352; UniProt 26–377 Author chain Cc; PDBConstruct 1–352; UniProt 26–377 Author chain Cd; PDBConstruct 1–352; UniProt 26–377 Author chain Ce; PDBConstruct 1–352; UniProt 26–377 Author chain Cf; PDBConstruct 1–352; UniProt 26–377 Author chain Cg; PDBConstruct 1–352; UniProt 26–377 Author chain Ch; PDBConstruct 1–352; UniProt 26–377 Author chain Ci; PDBConstruct 1–352; UniProt 26–377 Author chain Cj; PDBConstruct 1–352; UniProt 26–377 Author chain Ck; PDBConstruct 1–352; UniProt 26–377 Author chain Cl; PDBConstruct 1–352; UniProt 26–377 Author chain Cm; PDBConstruct 1–352; UniProt 26–377 Author chain Cn; PDBConstruct 1–352; UniProt 26–377 Author chain Co; PDBConstruct 1–352; UniProt 26–377 Author chain Cp; PDBConstruct 1–352; UniProt 26–377 Author chain Cq; PDBConstruct 1–352; UniProt 26–377 Author chain Cr; PDBConstruct 1–352; UniProt 26–377 Author chain Cs; PDBConstruct 1–352; UniProt 26–377 Author chain Ct; PDBConstruct 1–352; UniProt 26–377 Author chain Cu; PDBConstruct 1–352; UniProt 26–377 Author chain Cv; PDBConstruct 1–352; UniProt 26–377 Author chain Cw; PDBConstruct 1–352; UniProt 26–377 Author chain Cx; PDBConstruct 1–352; UniProt 26–377 Author chain Cy; PDBConstruct 1–352; UniProt 26–377 Author chain Cz; PDBConstruct 1–352; UniProt 26–377

Sodium-type flagellar protein MotY

Vibrio cholerae O1 biovar El Tor str. N16961

UniProt Q9KT95

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 × 298 PDB declaration: 298-meric(298) Consistent with protein copy count Chain Da; UniProt 23–293 Chain Db; UniProt 23–293 Chain Dc; UniProt 23–293 Chain Dd; UniProt 23–293 Chain De; UniProt 23–293 Chain Df; UniProt 23–293 Chain Dg; UniProt 23–293 Chain Dh; UniProt 23–293 Chain Di; UniProt 23–293 Chain Dj; UniProt 23–293 Chain Dk; UniProt 23–293 Chain Dl; UniProt 23–293 Chain Dm; UniProt 23–293 Chain Dn; UniProt 23–293 Chain Do; UniProt 23–293 Chain Dp; UniProt 23–293 Chain Dq; UniProt 23–293 Chain Dr; UniProt 23–293 Chain Ds; UniProt 23–293 Chain Dt; UniProt 23–293 Chain Du; UniProt 23–293 Chain Dv; UniProt 23–293 Chain Dw; UniProt 23–293 Chain Dx; UniProt 23–293 Chain Dy; UniProt 23–293 Chain Dz; UniProt 23–293 Not recorded Flagellar L-ring protein × 26 (Q9KQ13) Flagellar P-ring protein × 26 (Q9KQ14) Flagellar protein FlgT × 26 (Q9KPZ9) Sodium-type flagellar protein MotX × 26 (Q9KNX9) FlgP × 52 Lipoprotein × 58 (Q9KQ01) FlgO domain-containing protein × 58 (Q9KQ00) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.55 Å

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9KT95_VIBCH
Isoform
PDB entities 4
Chains and sequence ranges Author chain Da; PDBConstruct 1–271; UniProt 23–293 Author chain Db; PDBConstruct 1–271; UniProt 23–293 Author chain Dc; PDBConstruct 1–271; UniProt 23–293 Author chain Dd; PDBConstruct 1–271; UniProt 23–293 Author chain De; PDBConstruct 1–271; UniProt 23–293 Author chain Df; PDBConstruct 1–271; UniProt 23–293 Author chain Dg; PDBConstruct 1–271; UniProt 23–293 Author chain Dh; PDBConstruct 1–271; UniProt 23–293 Author chain Di; PDBConstruct 1–271; UniProt 23–293 Author chain Dj; PDBConstruct 1–271; UniProt 23–293 Author chain Dk; PDBConstruct 1–271; UniProt 23–293 Author chain Dl; PDBConstruct 1–271; UniProt 23–293 Author chain Dm; PDBConstruct 1–271; UniProt 23–293 Author chain Dn; PDBConstruct 1–271; UniProt 23–293 Author chain Do; PDBConstruct 1–271; UniProt 23–293 Author chain Dp; PDBConstruct 1–271; UniProt 23–293 Author chain Dq; PDBConstruct 1–271; UniProt 23–293 Author chain Dr; PDBConstruct 1–271; UniProt 23–293 Author chain Ds; PDBConstruct 1–271; UniProt 23–293 Author chain Dt; PDBConstruct 1–271; UniProt 23–293 Author chain Du; PDBConstruct 1–271; UniProt 23–293 Author chain Dv; PDBConstruct 1–271; UniProt 23–293 Author chain Dw; PDBConstruct 1–271; UniProt 23–293 Author chain Dx; PDBConstruct 1–271; UniProt 23–293 Author chain Dy; PDBConstruct 1–271; UniProt 23–293 Author chain Dz; PDBConstruct 1–271; UniProt 23–293

Sodium-type flagellar protein MotX

Vibrio cholerae O1 biovar El Tor str. N16961

UniProt Q9KNX9

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 × 298 PDB declaration: 298-meric(298) Consistent with protein copy count Chain Ea; UniProt 29–211 Chain Eb; UniProt 29–211 Chain Ec; UniProt 29–211 Chain Ed; UniProt 29–211 Chain Ee; UniProt 29–211 Chain Ef; UniProt 29–211 Chain Eg; UniProt 29–211 Chain Eh; UniProt 29–211 Chain Ei; UniProt 29–211 Chain Ej; UniProt 29–211 Chain Ek; UniProt 29–211 Chain El; UniProt 29–211 Chain Em; UniProt 29–211 Chain En; UniProt 29–211 Chain Eo; UniProt 29–211 Chain Ep; UniProt 29–211 Chain Eq; UniProt 29–211 Chain Er; UniProt 29–211 Chain Es; UniProt 29–211 Chain Et; UniProt 29–211 Chain Eu; UniProt 29–211 Chain Ev; UniProt 29–211 Chain Ew; UniProt 29–211 Chain Ex; UniProt 29–211 Chain Ey; UniProt 29–211 Chain Ez; UniProt 29–211 Not recorded Flagellar L-ring protein × 26 (Q9KQ13) Flagellar P-ring protein × 26 (Q9KQ14) Flagellar protein FlgT × 26 (Q9KPZ9) Sodium-type flagellar protein MotY × 26 (Q9KT95) FlgP × 52 Lipoprotein × 58 (Q9KQ01) FlgO domain-containing protein × 58 (Q9KQ00) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.55 Å

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9KNX9_VIBCH
Isoform
PDB entities 5
Chains and sequence ranges Author chain Ea; PDBConstruct 1–183; UniProt 29–211 Author chain Eb; PDBConstruct 1–183; UniProt 29–211 Author chain Ec; PDBConstruct 1–183; UniProt 29–211 Author chain Ed; PDBConstruct 1–183; UniProt 29–211 Author chain Ee; PDBConstruct 1–183; UniProt 29–211 Author chain Ef; PDBConstruct 1–183; UniProt 29–211 Author chain Eg; PDBConstruct 1–183; UniProt 29–211 Author chain Eh; PDBConstruct 1–183; UniProt 29–211 Author chain Ei; PDBConstruct 1–183; UniProt 29–211 Author chain Ej; PDBConstruct 1–183; UniProt 29–211 Author chain Ek; PDBConstruct 1–183; UniProt 29–211 Author chain El; PDBConstruct 1–183; UniProt 29–211 Author chain Em; PDBConstruct 1–183; UniProt 29–211 Author chain En; PDBConstruct 1–183; UniProt 29–211 Author chain Eo; PDBConstruct 1–183; UniProt 29–211 Author chain Ep; PDBConstruct 1–183; UniProt 29–211 Author chain Eq; PDBConstruct 1–183; UniProt 29–211 Author chain Er; PDBConstruct 1–183; UniProt 29–211 Author chain Es; PDBConstruct 1–183; UniProt 29–211 Author chain Et; PDBConstruct 1–183; UniProt 29–211 Author chain Eu; PDBConstruct 1–183; UniProt 29–211 Author chain Ev; PDBConstruct 1–183; UniProt 29–211 Author chain Ew; PDBConstruct 1–183; UniProt 29–211 Author chain Ex; PDBConstruct 1–183; UniProt 29–211 Author chain Ey; PDBConstruct 1–183; UniProt 29–211 Author chain Ez; PDBConstruct 1–183; UniProt 29–211

Lipoprotein

Vibrio cholerae O1 biovar El Tor str. N16961

UniProt Q9KQ01

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 × 298 PDB declaration: 298-meric(298) Consistent with protein copy count Chain Ha; UniProt 26–130 Chain Hc; UniProt 26–130 Chain He; UniProt 26–130 Chain Hg; UniProt 26–130 Chain Hi; UniProt 26–130 Chain Hk; UniProt 26–130 Chain Hm; UniProt 26–130 Chain Ho; UniProt 26–130 Chain Hq; UniProt 26–130 Chain Hs; UniProt 26–130 Chain Hu; UniProt 26–130 Chain Hw; UniProt 26–130 Chain Hy; UniProt 26–130 Chain Ia; UniProt 26–130 Chain Ic; UniProt 26–130 Chain Ie; UniProt 26–130 Chain Ig; UniProt 26–130 Chain Ii; UniProt 26–130 Chain Ik; UniProt 26–130 Chain Im; UniProt 26–130 Chain Io; UniProt 26–130 Chain Iq; UniProt 26–130 Chain Is; UniProt 26–130 Chain Iu; UniProt 26–130 Chain Iw; UniProt 26–130 Chain Iy; UniProt 26–130 Chain Ja; UniProt 26–130 Chain Jc; UniProt 26–130 Chain Je; UniProt 26–130 Chain Jg; UniProt 26–130 Chain Ji; UniProt 26–130 Chain Jk; UniProt 26–130 Chain Jm; UniProt 26–130 Chain Jo; UniProt 26–130 Chain Jq; UniProt 26–130 Chain Js; UniProt 26–130 Chain Ju; UniProt 26–130 Chain Jw; UniProt 26–130 Chain Jy; UniProt 26–130 Chain Ka; UniProt 26–130 Chain Kc; UniProt 26–130 Chain Ke; UniProt 26–130 Chain Kg; UniProt 26–130 Chain Ki; UniProt 26–130 Chain Kk; UniProt 26–130 Chain Km; UniProt 26–130 Chain Ko; UniProt 26–130 Chain Kq; UniProt 26–130 Chain Ks; UniProt 26–130 Chain Ku; UniProt 26–130 Chain Kw; UniProt 26–130 Chain Ky; UniProt 26–130 Chain La; UniProt 26–130 Chain Lc; UniProt 26–130 Chain Le; UniProt 26–130 Chain Lg; UniProt 26–130 Chain Li; UniProt 26–130 Chain Lk; UniProt 26–130 Not recorded Flagellar L-ring protein × 26 (Q9KQ13) Flagellar P-ring protein × 26 (Q9KQ14) Flagellar protein FlgT × 26 (Q9KPZ9) Sodium-type flagellar protein MotY × 26 (Q9KT95) Sodium-type flagellar protein MotX × 26 (Q9KNX9) FlgP × 52 FlgO domain-containing protein × 58 (Q9KQ00) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.55 Å

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9KQ01_VIBCH
Isoform
PDB entities 7
Chains and sequence ranges Author chain Ha; PDBConstruct 1–105; UniProt 26–130 Author chain Hc; PDBConstruct 1–105; UniProt 26–130 Author chain He; PDBConstruct 1–105; UniProt 26–130 Author chain Hg; PDBConstruct 1–105; UniProt 26–130 Author chain Hi; PDBConstruct 1–105; UniProt 26–130 Author chain Hk; PDBConstruct 1–105; UniProt 26–130 Author chain Hm; PDBConstruct 1–105; UniProt 26–130 Author chain Ho; PDBConstruct 1–105; UniProt 26–130 Author chain Hq; PDBConstruct 1–105; UniProt 26–130 Author chain Hs; PDBConstruct 1–105; UniProt 26–130 Author chain Hu; PDBConstruct 1–105; UniProt 26–130 Author chain Hw; PDBConstruct 1–105; UniProt 26–130 Author chain Hy; PDBConstruct 1–105; UniProt 26–130 Author chain Ia; PDBConstruct 1–105; UniProt 26–130 Author chain Ic; PDBConstruct 1–105; UniProt 26–130 Author chain Ie; PDBConstruct 1–105; UniProt 26–130 Author chain Ig; PDBConstruct 1–105; UniProt 26–130 Author chain Ii; PDBConstruct 1–105; UniProt 26–130 Author chain Ik; PDBConstruct 1–105; UniProt 26–130 Author chain Im; PDBConstruct 1–105; UniProt 26–130 Author chain Io; PDBConstruct 1–105; UniProt 26–130 Author chain Iq; PDBConstruct 1–105; UniProt 26–130 Author chain Is; PDBConstruct 1–105; UniProt 26–130 Author chain Iu; PDBConstruct 1–105; UniProt 26–130 Author chain Iw; PDBConstruct 1–105; UniProt 26–130 Author chain Iy; PDBConstruct 1–105; UniProt 26–130 Author chain Ja; PDBConstruct 1–105; UniProt 26–130 Author chain Jc; PDBConstruct 1–105; UniProt 26–130 Author chain Je; PDBConstruct 1–105; UniProt 26–130 Author chain Jg; PDBConstruct 1–105; UniProt 26–130 Author chain Ji; PDBConstruct 1–105; UniProt 26–130 Author chain Jk; PDBConstruct 1–105; UniProt 26–130 Author chain Jm; PDBConstruct 1–105; UniProt 26–130 Author chain Jo; PDBConstruct 1–105; UniProt 26–130 Author chain Jq; PDBConstruct 1–105; UniProt 26–130 Author chain Js; PDBConstruct 1–105; UniProt 26–130 Author chain Ju; PDBConstruct 1–105; UniProt 26–130 Author chain Jw; PDBConstruct 1–105; UniProt 26–130 Author chain Jy; PDBConstruct 1–105; UniProt 26–130 Author chain Ka; PDBConstruct 1–105; UniProt 26–130 Author chain Kc; PDBConstruct 1–105; UniProt 26–130 Author chain Ke; PDBConstruct 1–105; UniProt 26–130 Author chain Kg; PDBConstruct 1–105; UniProt 26–130 Author chain Ki; PDBConstruct 1–105; UniProt 26–130 Author chain Kk; PDBConstruct 1–105; UniProt 26–130 Author chain Km; PDBConstruct 1–105; UniProt 26–130 Author chain Ko; PDBConstruct 1–105; UniProt 26–130 Author chain Kq; PDBConstruct 1–105; UniProt 26–130 Author chain Ks; PDBConstruct 1–105; UniProt 26–130 Author chain Ku; PDBConstruct 1–105; UniProt 26–130 Author chain Kw; PDBConstruct 1–105; UniProt 26–130 Author chain Ky; PDBConstruct 1–105; UniProt 26–130 Author chain La; PDBConstruct 1–105; UniProt 26–130 Author chain Lc; PDBConstruct 1–105; UniProt 26–130 Author chain Le; PDBConstruct 1–105; UniProt 26–130 Author chain Lg; PDBConstruct 1–105; UniProt 26–130 Author chain Li; PDBConstruct 1–105; UniProt 26–130 Author chain Lk; PDBConstruct 1–105; UniProt 26–130

FlgO domain-containing protein

Vibrio cholerae O1 biovar El Tor str. N16961

UniProt Q9KQ00

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 × 298 PDB declaration: 298-meric(298) Consistent with protein copy count Chain Hb; UniProt 32–221 Chain Hd; UniProt 32–221 Chain Hf; UniProt 32–221 Chain Hh; UniProt 32–221 Chain Hj; UniProt 32–221 Chain Hl; UniProt 32–221 Chain Hn; UniProt 32–221 Chain Hp; UniProt 32–221 Chain Hr; UniProt 32–221 Chain Ht; UniProt 32–221 Chain Hv; UniProt 32–221 Chain Hx; UniProt 32–221 Chain Hz; UniProt 32–221 Chain Ib; UniProt 32–221 Chain Id; UniProt 32–221 Chain If; UniProt 32–221 Chain Ih; UniProt 32–221 Chain Ij; UniProt 32–221 Chain Il; UniProt 32–221 Chain In; UniProt 32–221 Chain Ip; UniProt 32–221 Chain Ir; UniProt 32–221 Chain It; UniProt 32–221 Chain Iv; UniProt 32–221 Chain Ix; UniProt 32–221 Chain Iz; UniProt 32–221 Chain Jb; UniProt 32–221 Chain Jd; UniProt 32–221 Chain Jf; UniProt 32–221 Chain Jh; UniProt 32–221 Chain Jj; UniProt 32–221 Chain Jl; UniProt 32–221 Chain Jn; UniProt 32–221 Chain Jp; UniProt 32–221 Chain Jr; UniProt 32–221 Chain Jt; UniProt 32–221 Chain Jv; UniProt 32–221 Chain Jx; UniProt 32–221 Chain Jz; UniProt 32–221 Chain Kb; UniProt 32–221 Chain Kd; UniProt 32–221 Chain Kf; UniProt 32–221 Chain Kh; UniProt 32–221 Chain Kj; UniProt 32–221 Chain Kl; UniProt 32–221 Chain Kn; UniProt 32–221 Chain Kp; UniProt 32–221 Chain Kr; UniProt 32–221 Chain Kt; UniProt 32–221 Chain Kv; UniProt 32–221 Chain Kx; UniProt 32–221 Chain Kz; UniProt 32–221 Chain Lb; UniProt 32–221 Chain Ld; UniProt 32–221 Chain Lf; UniProt 32–221 Chain Lh; UniProt 32–221 Chain Lj; UniProt 32–221 Chain Ll; UniProt 32–221 Not recorded Flagellar L-ring protein × 26 (Q9KQ13) Flagellar P-ring protein × 26 (Q9KQ14) Flagellar protein FlgT × 26 (Q9KPZ9) Sodium-type flagellar protein MotY × 26 (Q9KT95) Sodium-type flagellar protein MotX × 26 (Q9KNX9) FlgP × 52 Lipoprotein × 58 (Q9KQ01) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.55 Å

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9KQ00_VIBCH
Isoform
PDB entities 8
Chains and sequence ranges Author chain Hb; PDBConstruct 1–190; UniProt 32–221 Author chain Hd; PDBConstruct 1–190; UniProt 32–221 Author chain Hf; PDBConstruct 1–190; UniProt 32–221 Author chain Hh; PDBConstruct 1–190; UniProt 32–221 Author chain Hj; PDBConstruct 1–190; UniProt 32–221 Author chain Hl; PDBConstruct 1–190; UniProt 32–221 Author chain Hn; PDBConstruct 1–190; UniProt 32–221 Author chain Hp; PDBConstruct 1–190; UniProt 32–221 Author chain Hr; PDBConstruct 1–190; UniProt 32–221 Author chain Ht; PDBConstruct 1–190; UniProt 32–221 Author chain Hv; PDBConstruct 1–190; UniProt 32–221 Author chain Hx; PDBConstruct 1–190; UniProt 32–221 Author chain Hz; PDBConstruct 1–190; UniProt 32–221 Author chain Ib; PDBConstruct 1–190; UniProt 32–221 Author chain Id; PDBConstruct 1–190; UniProt 32–221 Author chain If; PDBConstruct 1–190; UniProt 32–221 Author chain Ih; PDBConstruct 1–190; UniProt 32–221 Author chain Ij; PDBConstruct 1–190; UniProt 32–221 Author chain Il; PDBConstruct 1–190; UniProt 32–221 Author chain In; PDBConstruct 1–190; UniProt 32–221 Author chain Ip; PDBConstruct 1–190; UniProt 32–221 Author chain Ir; PDBConstruct 1–190; UniProt 32–221 Author chain It; PDBConstruct 1–190; UniProt 32–221 Author chain Iv; PDBConstruct 1–190; UniProt 32–221 Author chain Ix; PDBConstruct 1–190; UniProt 32–221 Author chain Iz; PDBConstruct 1–190; UniProt 32–221 Author chain Jb; PDBConstruct 1–190; UniProt 32–221 Author chain Jd; PDBConstruct 1–190; UniProt 32–221 Author chain Jf; PDBConstruct 1–190; UniProt 32–221 Author chain Jh; PDBConstruct 1–190; UniProt 32–221 Author chain Jj; PDBConstruct 1–190; UniProt 32–221 Author chain Jl; PDBConstruct 1–190; UniProt 32–221 Author chain Jn; PDBConstruct 1–190; UniProt 32–221 Author chain Jp; PDBConstruct 1–190; UniProt 32–221 Author chain Jr; PDBConstruct 1–190; UniProt 32–221 Author chain Jt; PDBConstruct 1–190; UniProt 32–221 Author chain Jv; PDBConstruct 1–190; UniProt 32–221 Author chain Jx; PDBConstruct 1–190; UniProt 32–221 Author chain Jz; PDBConstruct 1–190; UniProt 32–221 Author chain Kb; PDBConstruct 1–190; UniProt 32–221 Author chain Kd; PDBConstruct 1–190; UniProt 32–221 Author chain Kf; PDBConstruct 1–190; UniProt 32–221 Author chain Kh; PDBConstruct 1–190; UniProt 32–221 Author chain Kj; PDBConstruct 1–190; UniProt 32–221 Author chain Kl; PDBConstruct 1–190; UniProt 32–221 Author chain Kn; PDBConstruct 1–190; UniProt 32–221 Author chain Kp; PDBConstruct 1–190; UniProt 32–221 Author chain Kr; PDBConstruct 1–190; UniProt 32–221 Author chain Kt; PDBConstruct 1–190; UniProt 32–221 Author chain Kv; PDBConstruct 1–190; UniProt 32–221 Author chain Kx; PDBConstruct 1–190; UniProt 32–221 Author chain Kz; PDBConstruct 1–190; UniProt 32–221 Author chain Lb; PDBConstruct 1–190; UniProt 32–221 Author chain Ld; PDBConstruct 1–190; UniProt 32–221 Author chain Lf; PDBConstruct 1–190; UniProt 32–221 Author chain Lh; PDBConstruct 1–190; UniProt 32–221 Author chain Lj; PDBConstruct 1–190; UniProt 32–221 Author chain Ll; PDBConstruct 1–190; UniProt 32–221

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 9yfg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yfg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9yfg
Deposition date deposition_date2025-09-25
Structure title titleFlagellar outer membrane complex in Vibrio cholerae at disassembled, closed state
Keywords keywordsVibrio cholerae, in situ cryo-EM, closed, flagellar outer membrane complex, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron152.40
Forward intensity I(0) i0487519000000.00
Molecular weight molecular_weight5869400.0 kDa
Excluded volume excluded_volume7299400 ų
Envelope volume envelope_volume12915000 ų
Hydration-shell volume shell_volume670530 ų
Envelope diameter envelope_diameter453.9
Shell Rg shell_rg150.40
Envelope Rg envelope_rg147.80
Shape Rg shape_rg152.40
Total Rg total_rg152.30
Total atoms total_atoms412635
Residues n_residues52997
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 dmax491.3
Rg (real space) rg_real155.10
Rg uncertainty (real space) rg_real_error3.14
I(0) (real space) i0_real4.8010e+11
I(0) uncertainty (real space) i0_real_error1.2370e+10
Rg (reciprocal space) rg_reciprocal143.60
I(0) (reciprocal space) i0_reciprocal460500000000.0000
Solution quality estimate total_estimate0.8897
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary147.4
Skewness Skewness skewness0.201
Kurtosis Kurtosis kurtosis-0.661
Angular range angular_range— – 0.0500 −1
Current regularization parameter α current_alpha1.5900
Highest regularization parameter α highest_alpha19010000000.0000
Real-space data points n_real_points11
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.972; Stabil: 0.906; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)