8wl2

Cryo-EM structure of the membrane-anchored part of the flagellar motor-hook complex in the CW state.

Method: ELECTRON MICROSCOPY Dmax: 396.2 Å Quality: GOOD

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

Flagellar L-ring protein

OrganismNot specified

UniProt P0A1N8

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 × 213 PDB declaration: 213-meric(213) Consistent with protein copy count Chain A; UniProt 1–232 Chain B; UniProt 1–232 Chain C; UniProt 1–232 Chain D; UniProt 1–232 Chain E; UniProt 1–232 Chain F; UniProt 1–232 Chain G; UniProt 1–232 Chain H; UniProt 1–232 Chain I; UniProt 1–232 Chain J; UniProt 1–232 Chain K; UniProt 1–232 Chain L; UniProt 1–232 Chain M; UniProt 1–232 Chain N; UniProt 1–232 Chain O; UniProt 1–232 Chain P; UniProt 1–232 Chain Q; UniProt 1–232 Chain R; UniProt 1–232 Chain S; UniProt 1–232 Chain T; UniProt 1–232 Chain U; UniProt 1–232 Chain V; UniProt 1–232 Chain W; UniProt 1–232 Chain X; UniProt 1–232 Chain Y; UniProt 1–232 Chain Z; UniProt 1–232 Not recorded Flagellar P-ring protein × 26 (P15930) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar M-ring protein × 76 (P15928) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.40 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGH_SALTY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–232; UniProt 1–232 Author chain B; PDBConstruct 1–232; UniProt 1–232 Author chain C; PDBConstruct 1–232; UniProt 1–232 Author chain D; PDBConstruct 1–232; UniProt 1–232 Author chain E; PDBConstruct 1–232; UniProt 1–232 Author chain F; PDBConstruct 1–232; UniProt 1–232 Author chain G; PDBConstruct 1–232; UniProt 1–232 Author chain H; PDBConstruct 1–232; UniProt 1–232 Author chain I; PDBConstruct 1–232; UniProt 1–232 Author chain J; PDBConstruct 1–232; UniProt 1–232 Author chain K; PDBConstruct 1–232; UniProt 1–232 Author chain L; PDBConstruct 1–232; UniProt 1–232 Author chain M; PDBConstruct 1–232; UniProt 1–232 Author chain N; PDBConstruct 1–232; UniProt 1–232 Author chain O; PDBConstruct 1–232; UniProt 1–232 Author chain P; PDBConstruct 1–232; UniProt 1–232 Author chain Q; PDBConstruct 1–232; UniProt 1–232 Author chain R; PDBConstruct 1–232; UniProt 1–232 Author chain S; PDBConstruct 1–232; UniProt 1–232 Author chain T; PDBConstruct 1–232; UniProt 1–232 Author chain U; PDBConstruct 1–232; UniProt 1–232 Author chain V; PDBConstruct 1–232; UniProt 1–232 Author chain W; PDBConstruct 1–232; UniProt 1–232 Author chain X; PDBConstruct 1–232; UniProt 1–232 Author chain Y; PDBConstruct 1–232; UniProt 1–232 Author chain Z; PDBConstruct 1–232; UniProt 1–232

Flagellar P-ring protein

OrganismNot specified

UniProt P15930

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 × 213 PDB declaration: 213-meric(213) Consistent with protein copy count Chain a; UniProt 1–365 Chain b; UniProt 1–365 Chain c; UniProt 1–365 Chain d; UniProt 1–365 Chain e; UniProt 1–365 Chain f; UniProt 1–365 Chain g; UniProt 1–365 Chain h; UniProt 1–365 Chain i; UniProt 1–365 Chain j; UniProt 1–365 Chain k; UniProt 1–365 Chain l; UniProt 1–365 Chain m; UniProt 1–365 Chain n; UniProt 1–365 Chain o; UniProt 1–365 Chain p; UniProt 1–365 Chain q; UniProt 1–365 Chain r; UniProt 1–365 Chain s; UniProt 1–365 Chain t; UniProt 1–365 Chain u; UniProt 1–365 Chain v; UniProt 1–365 Chain w; UniProt 1–365 Chain x; UniProt 1–365 Chain y; UniProt 1–365 Chain z; UniProt 1–365 Not recorded Flagellar L-ring protein × 26 (P0A1N8) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar M-ring protein × 76 (P15928) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.40 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGI_SALTY
Isoform
PDB entities 2
Chains and sequence ranges Author chain a; PDBConstruct 1–365; UniProt 1–365 Author chain b; PDBConstruct 1–365; UniProt 1–365 Author chain c; PDBConstruct 1–365; UniProt 1–365 Author chain d; PDBConstruct 1–365; UniProt 1–365 Author chain e; PDBConstruct 1–365; UniProt 1–365 Author chain f; PDBConstruct 1–365; UniProt 1–365 Author chain g; PDBConstruct 1–365; UniProt 1–365 Author chain h; PDBConstruct 1–365; UniProt 1–365 Author chain i; PDBConstruct 1–365; UniProt 1–365 Author chain j; PDBConstruct 1–365; UniProt 1–365 Author chain k; PDBConstruct 1–365; UniProt 1–365 Author chain l; PDBConstruct 1–365; UniProt 1–365 Author chain m; PDBConstruct 1–365; UniProt 1–365 Author chain n; PDBConstruct 1–365; UniProt 1–365 Author chain o; PDBConstruct 1–365; UniProt 1–365 Author chain p; PDBConstruct 1–365; UniProt 1–365 Author chain q; PDBConstruct 1–365; UniProt 1–365 Author chain r; PDBConstruct 1–365; UniProt 1–365 Author chain s; PDBConstruct 1–365; UniProt 1–365 Author chain t; PDBConstruct 1–365; UniProt 1–365 Author chain u; PDBConstruct 1–365; UniProt 1–365 Author chain v; PDBConstruct 1–365; UniProt 1–365 Author chain w; PDBConstruct 1–365; UniProt 1–365 Author chain x; PDBConstruct 1–365; UniProt 1–365 Author chain y; PDBConstruct 1–365; UniProt 1–365 Author chain z; PDBConstruct 1–365; UniProt 1–365

Flagellar basal-body rod protein FlgG

OrganismNot specified

UniProt P0A1J3

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 × 213 PDB declaration: 213-meric(213) Consistent with protein copy count Chain 0; UniProt 1–260 Chain 1; UniProt 1–260 Chain 2; UniProt 1–260 Chain 3; UniProt 1–260 Chain 4; UniProt 1–260 Chain 5; UniProt 1–260 Chain 6; UniProt 1–260 Chain 7; UniProt 1–260 Chain 8; UniProt 1–260 Chain 9; UniProt 1–260 Chain AF; UniProt 1–260 Chain AG; UniProt 1–260 Chain AH; UniProt 1–260 Chain AI; UniProt 1–260 Chain AJ; UniProt 1–260 Chain AK; UniProt 1–260 Chain AL; UniProt 1–260 Chain AM; UniProt 1–260 Chain AN; UniProt 1–260 Chain ZA; UniProt 1–260 Chain ZB; UniProt 1–260 Chain ZC; UniProt 1–260 Chain ZD; UniProt 1–260 Chain ZE; UniProt 1–260 Not recorded Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) Flagellar hook protein FlgE × 29 (P0A1J1) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar M-ring protein × 76 (P15928) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.40 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.

14 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGG_SALTY
Isoform
PDB entities 3
Chains and sequence ranges Author chain 0; PDBConstruct 1–260; UniProt 1–260 Author chain 1; PDBConstruct 1–260; UniProt 1–260 Author chain 2; PDBConstruct 1–260; UniProt 1–260 Author chain 3; PDBConstruct 1–260; UniProt 1–260 Author chain 4; PDBConstruct 1–260; UniProt 1–260 Author chain 5; PDBConstruct 1–260; UniProt 1–260 Author chain 6; PDBConstruct 1–260; UniProt 1–260 Author chain 7; PDBConstruct 1–260; UniProt 1–260 Author chain 8; PDBConstruct 1–260; UniProt 1–260 Author chain 9; PDBConstruct 1–260; UniProt 1–260 Author chain AF; PDBConstruct 1–260; UniProt 1–260 Author chain AG; PDBConstruct 1–260; UniProt 1–260 Author chain AH; PDBConstruct 1–260; UniProt 1–260 Author chain AI; PDBConstruct 1–260; UniProt 1–260 Author chain AJ; PDBConstruct 1–260; UniProt 1–260 Author chain AK; PDBConstruct 1–260; UniProt 1–260 Author chain AL; PDBConstruct 1–260; UniProt 1–260 Author chain AM; PDBConstruct 1–260; UniProt 1–260 Author chain AN; PDBConstruct 1–260; UniProt 1–260 Author chain ZA; PDBConstruct 1–260; UniProt 1–260 Author chain ZB; PDBConstruct 1–260; UniProt 1–260 Author chain ZC; PDBConstruct 1–260; UniProt 1–260 Author chain ZD; PDBConstruct 1–260; UniProt 1–260 Author chain ZE; PDBConstruct 1–260; UniProt 1–260

Flagellar hook protein FlgE

OrganismNot specified

UniProt P0A1J1

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 × 213 PDB declaration: 213-meric(213) Consistent with protein copy count Chain ZF; UniProt 1–403 Chain ZG; UniProt 1–403 Chain ZH; UniProt 1–403 Chain ZI; UniProt 1–403 Chain ZJ; UniProt 1–403 Chain ZK; UniProt 1–403 Chain ZL; UniProt 1–403 Chain ZM; UniProt 1–403 Chain ZN; UniProt 1–403 Chain ZO; UniProt 1–403 Chain ZP; UniProt 1–403 Chain ZQ; UniProt 1–403 Chain ZR; UniProt 1–403 Chain ZS; UniProt 1–403 Chain ZT; UniProt 1–403 Chain ZU; UniProt 1–403 Chain ZV; UniProt 1–403 Chain ZW; UniProt 1–403 Chain ZX; UniProt 1–403 Chain ZY; UniProt 1–403 Chain ZZ; UniProt 1–403 Chain Za; UniProt 1–403 Chain Zb; UniProt 1–403 Chain Zc; UniProt 1–403 Chain Zd; UniProt 1–403 Chain Ze; UniProt 1–403 Chain Zf; UniProt 1–403 Chain Zg; UniProt 1–403 Chain Zh; UniProt 1–403 Not recorded Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar M-ring protein × 76 (P15928) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.40 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.

20 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGE_SALTY
Isoform
PDB entities 4
Chains and sequence ranges Author chain ZF; PDBConstruct 1–403; UniProt 1–403 Author chain ZG; PDBConstruct 1–403; UniProt 1–403 Author chain ZH; PDBConstruct 1–403; UniProt 1–403 Author chain ZI; PDBConstruct 1–403; UniProt 1–403 Author chain ZJ; PDBConstruct 1–403; UniProt 1–403 Author chain ZK; PDBConstruct 1–403; UniProt 1–403 Author chain ZL; PDBConstruct 1–403; UniProt 1–403 Author chain ZM; PDBConstruct 1–403; UniProt 1–403 Author chain ZN; PDBConstruct 1–403; UniProt 1–403 Author chain ZO; PDBConstruct 1–403; UniProt 1–403 Author chain ZP; PDBConstruct 1–403; UniProt 1–403 Author chain ZQ; PDBConstruct 1–403; UniProt 1–403 Author chain ZR; PDBConstruct 1–403; UniProt 1–403 Author chain ZS; PDBConstruct 1–403; UniProt 1–403 Author chain ZT; PDBConstruct 1–403; UniProt 1–403 Author chain ZU; PDBConstruct 1–403; UniProt 1–403 Author chain ZV; PDBConstruct 1–403; UniProt 1–403 Author chain ZW; PDBConstruct 1–403; UniProt 1–403 Author chain ZX; PDBConstruct 1–403; UniProt 1–403 Author chain ZY; PDBConstruct 1–403; UniProt 1–403 Author chain ZZ; PDBConstruct 1–403; UniProt 1–403 Author chain Za; PDBConstruct 1–403; UniProt 1–403 Author chain Zb; PDBConstruct 1–403; UniProt 1–403 Author chain Zc; PDBConstruct 1–403; UniProt 1–403 Author chain Zd; PDBConstruct 1–403; UniProt 1–403 Author chain Ze; PDBConstruct 1–403; UniProt 1–403 Author chain Zf; PDBConstruct 1–403; UniProt 1–403 Author chain Zg; PDBConstruct 1–403; UniProt 1–403 Author chain Zh; PDBConstruct 1–403; UniProt 1–403

Flagellar basal-body rod protein FlgF

OrganismNot specified

UniProt P16323

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 × 213 PDB declaration: 213-meric(213) Consistent with protein copy count Chain AA; UniProt 1–251 Chain AB; UniProt 1–251 Chain AC; UniProt 1–251 Chain AD; UniProt 1–251 Chain AE; UniProt 1–251 Not recorded Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) Flagellar M-ring protein × 76 (P15928) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.40 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGF_SALTY
Isoform
PDB entities 5
Chains and sequence ranges Author chain AA; PDBConstruct 1–251; UniProt 1–251 Author chain AB; PDBConstruct 1–251; UniProt 1–251 Author chain AC; PDBConstruct 1–251; UniProt 1–251 Author chain AD; PDBConstruct 1–251; UniProt 1–251 Author chain AE; PDBConstruct 1–251; UniProt 1–251

Flagellar M-ring protein

OrganismNot specified

UniProt P15928

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 × 213 PDB declaration: 213-meric(213) Consistent with protein copy count Chain AO; UniProt 1–560 Chain AP; UniProt 1–560 Chain AQ; UniProt 1–560 Chain AR; UniProt 1–560 Chain AS; UniProt 1–560 Chain AT; UniProt 1–560 Chain AU; UniProt 1–560 Chain AV; UniProt 1–560 Chain AW; UniProt 1–560 Chain AX; UniProt 1–560 Chain AY; UniProt 1–560 Chain AZ; UniProt 1–560 Chain Aa; UniProt 1–560 Chain Ac; UniProt 1–560 Chain Ad; UniProt 1–560 Chain Ae; UniProt 1–560 Chain Af; UniProt 1–560 Chain Ag; UniProt 1–560 Chain Ah; UniProt 1–560 Chain Ai; UniProt 1–560 Chain Aj; UniProt 1–560 Chain Ak; UniProt 1–560 Chain Al; UniProt 1–560 Chain Am; UniProt 1–560 Chain An; UniProt 1–560 Chain Ao; UniProt 1–560 Chain Ap; UniProt 1–560 Chain BG; UniProt 1–560 Chain BH; UniProt 1–560 Chain BI; UniProt 1–560 Chain BJ; UniProt 1–560 Chain BK; UniProt 1–560 Chain BL; UniProt 1–560 Chain BM; UniProt 1–560 Chain BN; UniProt 1–560 Chain BO; UniProt 1–560 Chain BP; UniProt 1–560 Chain BQ; UniProt 1–560 Chain BR; UniProt 1–560 Chain BS; UniProt 1–560 Chain BT; UniProt 1–560 Chain BU; UniProt 1–560 Chain BV; UniProt 1–560 Chain BW; UniProt 1–560 Chain BX; UniProt 1–560 Chain UI; UniProt 1–560 Chain UJ; UniProt 1–560 Chain UK; UniProt 1–560 Chain UL; UniProt 1–560 Chain UM; UniProt 1–560 Chain UN; UniProt 1–560 Chain UO; UniProt 1–560 Chain UP; UniProt 1–560 Chain WA; UniProt 1–560 Chain WB; UniProt 1–560 Chain WC; UniProt 1–560 Chain WD; UniProt 1–560 Chain WE; UniProt 1–560 Chain WF; UniProt 1–560 Chain WG; UniProt 1–560 Chain WH; UniProt 1–560 Chain WI; UniProt 1–560 Chain WJ; UniProt 1–560 Chain WK; UniProt 1–560 Chain WL; UniProt 1–560 Chain WM; UniProt 1–560 Chain WN; UniProt 1–560 Chain WO; UniProt 1–560 Chain WP; UniProt 1–560 Chain WQ; UniProt 1–560 Chain WR; UniProt 1–560 Chain WS; UniProt 1–560 Chain WT; UniProt 1–560 Chain WU; UniProt 1–560 Chain WV; UniProt 1–560 Chain WW; UniProt 1–560 Not recorded Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.40 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.

47 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIF_SALTY
Isoform
PDB entities 6
Chains and sequence ranges 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 Author chain AZ; PDBConstruct 1–560; UniProt 1–560 Author chain Aa; 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 BG; PDBConstruct 1–560; UniProt 1–560 Author chain BH; PDBConstruct 1–560; UniProt 1–560 Author chain BI; PDBConstruct 1–560; UniProt 1–560 Author chain BJ; PDBConstruct 1–560; UniProt 1–560 Author chain BK; PDBConstruct 1–560; UniProt 1–560 Author chain BL; PDBConstruct 1–560; UniProt 1–560 Author chain BM; PDBConstruct 1–560; UniProt 1–560 Author chain BN; PDBConstruct 1–560; UniProt 1–560 Author chain BO; PDBConstruct 1–560; UniProt 1–560 Author chain BP; PDBConstruct 1–560; UniProt 1–560 Author chain BQ; PDBConstruct 1–560; UniProt 1–560 Author chain BR; PDBConstruct 1–560; UniProt 1–560 Author chain BS; PDBConstruct 1–560; UniProt 1–560 Author chain BT; PDBConstruct 1–560; UniProt 1–560 Author chain BU; PDBConstruct 1–560; UniProt 1–560 Author chain BV; PDBConstruct 1–560; UniProt 1–560 Author chain BW; PDBConstruct 1–560; UniProt 1–560 Author chain BX; PDBConstruct 1–560; UniProt 1–560 Author chain UI; PDBConstruct 1–560; UniProt 1–560 Author chain UJ; PDBConstruct 1–560; UniProt 1–560 Author chain UK; PDBConstruct 1–560; UniProt 1–560 Author chain UL; PDBConstruct 1–560; UniProt 1–560 Author chain UM; PDBConstruct 1–560; UniProt 1–560 Author chain UN; PDBConstruct 1–560; UniProt 1–560 Author chain UO; PDBConstruct 1–560; UniProt 1–560 Author chain UP; PDBConstruct 1–560; UniProt 1–560 Author chain WA; PDBConstruct 1–560; UniProt 1–560 Author chain WB; PDBConstruct 1–560; UniProt 1–560 Author chain WC; PDBConstruct 1–560; UniProt 1–560 Author chain WD; PDBConstruct 1–560; UniProt 1–560 Author chain WE; PDBConstruct 1–560; UniProt 1–560 Author chain WF; PDBConstruct 1–560; UniProt 1–560 Author chain WG; PDBConstruct 1–560; UniProt 1–560 Author chain WH; PDBConstruct 1–560; UniProt 1–560 Author chain WI; PDBConstruct 1–560; UniProt 1–560 Author chain WJ; PDBConstruct 1–560; UniProt 1–560 Author chain WK; PDBConstruct 1–560; UniProt 1–560 Author chain WL; PDBConstruct 1–560; UniProt 1–560 Author chain WM; PDBConstruct 1–560; UniProt 1–560 Author chain WN; PDBConstruct 1–560; UniProt 1–560 Author chain WO; PDBConstruct 1–560; UniProt 1–560 Author chain WP; PDBConstruct 1–560; UniProt 1–560 Author chain WQ; PDBConstruct 1–560; UniProt 1–560 Author chain WR; PDBConstruct 1–560; UniProt 1–560 Author chain WS; PDBConstruct 1–560; UniProt 1–560 Author chain WT; PDBConstruct 1–560; UniProt 1–560 Author chain WU; PDBConstruct 1–560; UniProt 1–560 Author chain WV; PDBConstruct 1–560; UniProt 1–560 Author chain WW; PDBConstruct 1–560; UniProt 1–560

Flagellar biosynthetic protein FliQ

OrganismNot specified

UniProt P0A1L5

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 × 213 PDB declaration: 213-meric(213) Consistent with protein copy count Chain Ab; UniProt 1–89 Chain Aq; UniProt 1–89 Chain Ar; UniProt 1–89 Chain As; UniProt 1–89 Not recorded Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar M-ring protein × 76 (P15928) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.40 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIQ_SALTY
Isoform
PDB entities 7
Chains and sequence ranges Author chain Ab; PDBConstruct 1–89; UniProt 1–89 Author chain Aq; PDBConstruct 1–89; UniProt 1–89 Author chain Ar; PDBConstruct 1–89; UniProt 1–89 Author chain As; PDBConstruct 1–89; UniProt 1–89

Flagellar biosynthetic protein FliR

OrganismNot specified

UniProt P54702

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 × 213 PDB declaration: 213-meric(213) Consistent with protein copy count Chain At; UniProt 1–264 Not recorded Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar M-ring protein × 76 (P15928) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.40 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIR_SALTY
Isoform
PDB entities 8
Chains and sequence ranges Author chain At; PDBConstruct 1–264; UniProt 1–264

Flagellar biosynthetic protein FliP

OrganismNot specified

UniProt P54700

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 × 213 PDB declaration: 213-meric(213) Consistent with protein copy count Chain Au; UniProt 1–245 Chain Av; UniProt 1–245 Chain Aw; UniProt 1–245 Chain Ax; UniProt 1–245 Chain Ay; UniProt 1–245 Not recorded Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar M-ring protein × 76 (P15928) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.40 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIP_SALTY
Isoform
PDB entities 9
Chains and sequence ranges Author chain Au; PDBConstruct 1–245; UniProt 1–245 Author chain Av; PDBConstruct 1–245; UniProt 1–245 Author chain Aw; PDBConstruct 1–245; UniProt 1–245 Author chain Ax; PDBConstruct 1–245; UniProt 1–245 Author chain Ay; PDBConstruct 1–245; UniProt 1–245

Flagellar hook-basal body complex protein FliE

OrganismNot specified

UniProt P26462

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 × 213 PDB declaration: 213-meric(213) Consistent with protein copy count Chain A1; UniProt 1–104 Chain A2; UniProt 1–104 Chain A3; UniProt 1–104 Chain A4; UniProt 1–104 Chain A5; UniProt 1–104 Chain Az; UniProt 1–104 Not recorded Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar M-ring protein × 76 (P15928) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.40 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIE_SALTY
Isoform
PDB entities 10
Chains and sequence ranges Author chain A1; PDBConstruct 1–104; UniProt 1–104 Author chain A2; PDBConstruct 1–104; UniProt 1–104 Author chain A3; PDBConstruct 1–104; UniProt 1–104 Author chain A4; PDBConstruct 1–104; UniProt 1–104 Author chain A5; PDBConstruct 1–104; UniProt 1–104 Author chain Az; PDBConstruct 1–104; UniProt 1–104

Flagellar basal body rod protein FlgB

OrganismNot specified

UniProt P16437

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 × 213 PDB declaration: 213-meric(213) Consistent with protein copy count Chain A0; UniProt 1–138 Chain A6; UniProt 1–138 Chain A7; UniProt 1–138 Chain A8; UniProt 1–138 Chain A9; UniProt 1–138 Not recorded Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar M-ring protein × 76 (P15928) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.40 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGB_SALTY
Isoform
PDB entities 11
Chains and sequence ranges Author chain A0; PDBConstruct 1–138; UniProt 1–138 Author chain A6; PDBConstruct 1–138; UniProt 1–138 Author chain A7; PDBConstruct 1–138; UniProt 1–138 Author chain A8; PDBConstruct 1–138; UniProt 1–138 Author chain A9; PDBConstruct 1–138; UniProt 1–138

Flagellar basal-body rod protein FlgC

OrganismNot specified

UniProt P0A1I7

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 × 213 PDB declaration: 213-meric(213) Consistent with protein copy count Chain BA; UniProt 1–134 Chain BB; UniProt 1–134 Chain BC; UniProt 1–134 Chain BD; UniProt 1–134 Chain BE; UniProt 1–134 Chain BF; UniProt 1–134 Not recorded Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar M-ring protein × 76 (P15928) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.40 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGC_SALTY
Isoform
PDB entities 12
Chains and sequence ranges Author chain BA; PDBConstruct 1–134; UniProt 1–134 Author chain BB; PDBConstruct 1–134; UniProt 1–134 Author chain BC; PDBConstruct 1–134; UniProt 1–134 Author chain BD; PDBConstruct 1–134; UniProt 1–134 Author chain BE; PDBConstruct 1–134; UniProt 1–134 Author chain BF; PDBConstruct 1–134; UniProt 1–134

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 8wl2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wl2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8wl2
Deposition date deposition_date2023-09-29
Structure title titleCryo-EM structure of the membrane-anchored part of the flagellar motor-hook complex in the CW state.
Keywords keywordsFlagellum, Flagellar motor, 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_electron135.60
Forward intensity I(0) i0338507000000.00
Molecular weight molecular_weight4821700.0 kDa
Excluded volume excluded_volume5973700 ų
Envelope volume envelope_volume10251000 ų
Hydration-shell volume shell_volume614780 ų
Envelope diameter envelope_diameter495.7
Shell Rg shell_rg128.60
Envelope Rg envelope_rg138.80
Shape Rg shape_rg135.60
Total Rg total_rg135.30
Total atoms total_atoms338677
Residues n_residues45378
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 dmax396.2
Rg (real space) rg_real129.50
Rg uncertainty (real space) rg_real_error1.90
I(0) (real space) i0_real3.2550e+11
I(0) uncertainty (real space) i0_real_error7.7380e+09
Rg (reciprocal space) rg_reciprocal121.80
I(0) (reciprocal space) i0_reciprocal323700000000.0000
Solution quality estimate total_estimate0.8932
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary144.1
Skewness Skewness skewness0.509
Kurtosis Kurtosis kurtosis-0.205
Angular range angular_range— – 0.0550 −1
Current regularization parameter α current_alpha1.2410
Highest regularization parameter α highest_alpha19640000000.0000
Real-space data points n_real_points12
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 0.938; Stabil: 0.965; Sysdev: 1.000; Positv: 1.000; Valcen: 0.903; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)