7cgo

Cryo-EM structure of the flagellar motor-hook complex from Salmonella

Method: ELECTRON MICROSCOPY Dmax: 397.7 Å Quality: GOOD

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

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 × 219 PDB declaration: 219-meric(219) Consistent with protein copy count Chain A; UniProt 1–260 Chain B; UniProt 1–260 Chain C; UniProt 1–260 Chain D; UniProt 1–260 Chain E; UniProt 1–260 Chain F; UniProt 1–260 Chain G; UniProt 1–260 Chain H; UniProt 1–260 Chain I; UniProt 1–260 Chain J; UniProt 1–260 Chain K; UniProt 1–260 Chain L; UniProt 1–260 Chain M; UniProt 1–260 Chain N; UniProt 1–260 Chain O; UniProt 1–260 Chain P; UniProt 1–260 Chain Q; UniProt 1–260 Chain R; UniProt 1–260 Chain S; UniProt 1–260 Chain T; UniProt 1–260 Chain U; UniProt 1–260 Chain V; UniProt 1–260 Chain W; UniProt 1–260 Chain X; UniProt 1–260 Not recorded Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 33 (P0A1J1) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar M-ring protein × 57 (P15928) FlgB-Dc loop × 5 FliE helix 1 × 6 Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.90 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–260; UniProt 1–260 Author chain B; PDBConstruct 1–260; UniProt 1–260 Author chain C; PDBConstruct 1–260; UniProt 1–260 Author chain D; PDBConstruct 1–260; UniProt 1–260 Author chain E; PDBConstruct 1–260; UniProt 1–260 Author chain F; PDBConstruct 1–260; UniProt 1–260 Author chain G; PDBConstruct 1–260; UniProt 1–260 Author chain H; PDBConstruct 1–260; UniProt 1–260 Author chain I; PDBConstruct 1–260; UniProt 1–260 Author chain J; PDBConstruct 1–260; UniProt 1–260 Author chain K; PDBConstruct 1–260; UniProt 1–260 Author chain L; PDBConstruct 1–260; UniProt 1–260 Author chain M; PDBConstruct 1–260; UniProt 1–260 Author chain N; PDBConstruct 1–260; UniProt 1–260 Author chain O; PDBConstruct 1–260; UniProt 1–260 Author chain P; PDBConstruct 1–260; UniProt 1–260 Author chain Q; PDBConstruct 1–260; UniProt 1–260 Author chain R; PDBConstruct 1–260; UniProt 1–260 Author chain S; PDBConstruct 1–260; UniProt 1–260 Author chain T; PDBConstruct 1–260; UniProt 1–260 Author chain U; PDBConstruct 1–260; UniProt 1–260 Author chain V; PDBConstruct 1–260; UniProt 1–260 Author chain W; PDBConstruct 1–260; UniProt 1–260 Author chain X; PDBConstruct 1–260; UniProt 1–260

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 × 219 PDB declaration: 219-meric(219) Consistent with protein copy count Chain a; UniProt 1–251 Chain b; UniProt 1–251 Chain c; UniProt 1–251 Chain d; UniProt 1–251 Chain e; UniProt 1–251 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 33 (P0A1J1) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar M-ring protein × 57 (P15928) FlgB-Dc loop × 5 FliE helix 1 × 6 Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.90 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 2
Chains and sequence ranges Author chain a; PDBConstruct 1–251; UniProt 1–251 Author chain b; PDBConstruct 1–251; UniProt 1–251 Author chain c; PDBConstruct 1–251; UniProt 1–251 Author chain d; PDBConstruct 1–251; UniProt 1–251 Author chain e; PDBConstruct 1–251; UniProt 1–251

Flagellar MS ring L1

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 × 219 PDB declaration: 219-meric(219) Consistent with protein copy count Chain 5; UniProt 311–331 Chain 6; UniProt 311–331 Chain 7; UniProt 311–331 Chain 8; UniProt 311–331 Chain 9; UniProt 311–331 Chain Ca; UniProt 1–560 Chain Cb; UniProt 1–560 Chain Cc; UniProt 1–560 Chain Cd; UniProt 1–560 Chain Ce; UniProt 1–560 Chain Cf; UniProt 1–560 Chain Cg; UniProt 1–560 Chain Ch; UniProt 1–560 Chain Ci; UniProt 1–560 Chain Cj; UniProt 1–560 Chain Ck; UniProt 1–560 Chain Cl; UniProt 1–560 Chain Cm; UniProt 1–560 Chain Cn; UniProt 1–560 Chain Co; UniProt 1–560 Chain Cp; UniProt 1–560 Chain Cq; UniProt 1–560 Chain Cr; UniProt 1–560 Chain Cs; UniProt 1–560 Chain Ct; UniProt 1–560 Chain Cu; UniProt 1–560 Chain Cv; UniProt 1–560 Chain Cw; UniProt 1–560 Chain Cx; UniProt 1–560 Chain Cy; UniProt 1–560 Chain Cz; UniProt 1–560 Chain Da; UniProt 1–560 Chain Db; UniProt 1–560 Chain Dc; UniProt 1–560 Chain Dd; UniProt 1–560 Chain De; UniProt 1–560 Chain Df; UniProt 1–560 Chain Dg; UniProt 1–560 Chain Dh; UniProt 1–560 Chain Di; UniProt 1–560 Chain Dj; UniProt 1–560 Chain Dk; UniProt 1–560 Chain Dl; UniProt 1–560 Chain Dm; UniProt 1–560 Chain Dn; UniProt 1–560 Chain Do; UniProt 1–560 Chain Dp; UniProt 1–560 Chain Dq; UniProt 1–560 Chain Dr; UniProt 1–560 Chain Ds; UniProt 1–560 Chain Dt; UniProt 1–560 Chain Du; UniProt 1–560 Chain Dv; UniProt 1–560 Chain Dw; UniProt 1–560 Chain Ea; UniProt 1–560 Chain Eb; UniProt 1–560 Chain Ec; UniProt 1–560 Chain Ed; UniProt 1–560 Chain Ee; UniProt 1–560 Chain Ef; UniProt 1–560 Chain Eg; UniProt 1–560 Chain Eh; UniProt 1–560 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 33 (P0A1J1) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) FlgB-Dc loop × 5 FliE helix 1 × 6 Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.90 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 4, 12
Chains and sequence ranges Author chain 5; PDBConstruct 1–21; UniProt 311–331 Author chain 6; PDBConstruct 1–21; UniProt 311–331 Author chain 7; PDBConstruct 1–21; UniProt 311–331 Author chain 8; PDBConstruct 1–21; UniProt 311–331 Author chain 9; PDBConstruct 1–21; UniProt 311–331 Author chain Ca; PDBConstruct 1–560; UniProt 1–560 Author chain Cb; PDBConstruct 1–560; UniProt 1–560 Author chain Cc; PDBConstruct 1–560; UniProt 1–560 Author chain Cd; PDBConstruct 1–560; UniProt 1–560 Author chain Ce; PDBConstruct 1–560; UniProt 1–560 Author chain Cf; PDBConstruct 1–560; UniProt 1–560 Author chain Cg; PDBConstruct 1–560; UniProt 1–560 Author chain Ch; PDBConstruct 1–560; UniProt 1–560 Author chain Ci; PDBConstruct 1–560; UniProt 1–560 Author chain Cj; PDBConstruct 1–560; UniProt 1–560 Author chain Ck; PDBConstruct 1–560; UniProt 1–560 Author chain Cl; PDBConstruct 1–560; UniProt 1–560 Author chain Cm; PDBConstruct 1–560; UniProt 1–560 Author chain Cn; PDBConstruct 1–560; UniProt 1–560 Author chain Co; PDBConstruct 1–560; UniProt 1–560 Author chain Cp; PDBConstruct 1–560; UniProt 1–560 Author chain Cq; PDBConstruct 1–560; UniProt 1–560 Author chain Cr; PDBConstruct 1–560; UniProt 1–560 Author chain Cs; PDBConstruct 1–560; UniProt 1–560 Author chain Ct; PDBConstruct 1–560; UniProt 1–560 Author chain Cu; PDBConstruct 1–560; UniProt 1–560 Author chain Cv; PDBConstruct 1–560; UniProt 1–560 Author chain Cw; PDBConstruct 1–560; UniProt 1–560 Author chain Cx; PDBConstruct 1–560; UniProt 1–560 Author chain Cy; PDBConstruct 1–560; UniProt 1–560 Author chain Cz; PDBConstruct 1–560; UniProt 1–560 Author chain Da; PDBConstruct 1–560; UniProt 1–560 Author chain Db; PDBConstruct 1–560; UniProt 1–560 Author chain Dc; PDBConstruct 1–560; UniProt 1–560 Author chain Dd; PDBConstruct 1–560; UniProt 1–560 Author chain De; PDBConstruct 1–560; UniProt 1–560 Author chain Df; PDBConstruct 1–560; UniProt 1–560 Author chain Dg; PDBConstruct 1–560; UniProt 1–560 Author chain Dh; PDBConstruct 1–560; UniProt 1–560 Author chain Di; PDBConstruct 1–560; UniProt 1–560 Author chain Dj; PDBConstruct 1–560; UniProt 1–560 Author chain Dk; PDBConstruct 1–560; UniProt 1–560 Author chain Dl; PDBConstruct 1–560; UniProt 1–560 Author chain Dm; PDBConstruct 1–560; UniProt 1–560 Author chain Dn; PDBConstruct 1–560; UniProt 1–560 Author chain Do; PDBConstruct 1–560; UniProt 1–560 Author chain Dp; PDBConstruct 1–560; UniProt 1–560 Author chain Dq; PDBConstruct 1–560; UniProt 1–560 Author chain Dr; PDBConstruct 1–560; UniProt 1–560 Author chain Ds; PDBConstruct 1–560; UniProt 1–560 Author chain Dt; PDBConstruct 1–560; UniProt 1–560 Author chain Du; PDBConstruct 1–560; UniProt 1–560 Author chain Dv; PDBConstruct 1–560; UniProt 1–560 Author chain Dw; PDBConstruct 1–560; UniProt 1–560 Author chain Ea; PDBConstruct 1–560; UniProt 1–560 Author chain Eb; PDBConstruct 1–560; UniProt 1–560 Author chain Ec; PDBConstruct 1–560; UniProt 1–560 Author chain Ed; PDBConstruct 1–560; UniProt 1–560 Author chain Ee; PDBConstruct 1–560; UniProt 1–560 Author chain Ef; PDBConstruct 1–560; UniProt 1–560 Author chain Eg; PDBConstruct 1–560; UniProt 1–560 Author chain Eh; PDBConstruct 1–560; UniProt 1–560

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 × 219 PDB declaration: 219-meric(219) Consistent with protein copy count Chain f; UniProt 1–134 Chain g; UniProt 1–134 Chain h; UniProt 1–134 Chain i; UniProt 1–134 Chain j; UniProt 1–134 Chain p; UniProt 1–134 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 33 (P0A1J1) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar M-ring protein × 57 (P15928) FlgB-Dc loop × 5 FliE helix 1 × 6 Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.90 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 5
Chains and sequence ranges Author chain f; PDBConstruct 1–134; UniProt 1–134 Author chain g; PDBConstruct 1–134; UniProt 1–134 Author chain h; PDBConstruct 1–134; UniProt 1–134 Author chain i; PDBConstruct 1–134; UniProt 1–134 Author chain j; PDBConstruct 1–134; UniProt 1–134 Author chain p; PDBConstruct 1–134; UniProt 1–134

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 × 219 PDB declaration: 219-meric(219) Consistent with protein copy count Chain k; UniProt 1–138 Chain l; UniProt 1–138 Chain m; UniProt 1–138 Chain n; UniProt 1–138 Chain o; UniProt 1–138 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 33 (P0A1J1) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar M-ring protein × 57 (P15928) FlgB-Dc loop × 5 FliE helix 1 × 6 Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.90 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 6
Chains and sequence ranges Author chain k; PDBConstruct 1–138; UniProt 1–138 Author chain l; PDBConstruct 1–138; UniProt 1–138 Author chain m; PDBConstruct 1–138; UniProt 1–138 Author chain n; PDBConstruct 1–138; UniProt 1–138 Author chain o; PDBConstruct 1–138; UniProt 1–138

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 × 219 PDB declaration: 219-meric(219) Consistent with protein copy count Chain q; UniProt 1–104 Chain r; UniProt 1–104 Chain s; UniProt 1–104 Chain t; UniProt 1–104 Chain u; UniProt 1–104 Chain v; UniProt 1–104 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook protein FlgE × 33 (P0A1J1) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar M-ring protein × 57 (P15928) FlgB-Dc loop × 5 FliE helix 1 × 6 Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.90 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 7
Chains and sequence ranges Author chain q; PDBConstruct 1–104; UniProt 1–104 Author chain r; PDBConstruct 1–104; UniProt 1–104 Author chain s; PDBConstruct 1–104; UniProt 1–104 Author chain t; PDBConstruct 1–104; UniProt 1–104 Author chain u; PDBConstruct 1–104; UniProt 1–104 Author chain v; PDBConstruct 1–104; UniProt 1–104

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 × 219 PDB declaration: 219-meric(219) Consistent with protein copy count Chain DA; UniProt 1–403 Chain DB; UniProt 1–403 Chain DC; UniProt 1–403 Chain DD; UniProt 1–403 Chain DE; UniProt 1–403 Chain DF; UniProt 1–403 Chain DG; UniProt 1–403 Chain DH; UniProt 1–403 Chain DI; UniProt 1–403 Chain DJ; UniProt 1–403 Chain DK; UniProt 1–403 Chain DL; UniProt 1–403 Chain DM; UniProt 1–403 Chain DN; UniProt 1–403 Chain DO; UniProt 1–403 Chain DP; UniProt 1–403 Chain DQ; UniProt 1–403 Chain DR; UniProt 1–403 Chain DS; UniProt 1–403 Chain DT; UniProt 1–403 Chain DU; UniProt 1–403 Chain DV; UniProt 1–403 Chain DW; UniProt 1–403 Chain DX; UniProt 1–403 Chain DY; UniProt 1–403 Chain DZ; UniProt 1–403 Chain EA; UniProt 1–403 Chain EB; UniProt 1–403 Chain EC; UniProt 1–403 Chain ED; UniProt 1–403 Chain EE; UniProt 1–403 Chain EF; UniProt 1–403 Chain EG; UniProt 1–403 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar M-ring protein × 57 (P15928) FlgB-Dc loop × 5 FliE helix 1 × 6 Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.90 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 8
Chains and sequence ranges Author chain DA; PDBConstruct 1–403; UniProt 1–403 Author chain DB; PDBConstruct 1–403; UniProt 1–403 Author chain DC; PDBConstruct 1–403; UniProt 1–403 Author chain DD; PDBConstruct 1–403; UniProt 1–403 Author chain DE; PDBConstruct 1–403; UniProt 1–403 Author chain DF; PDBConstruct 1–403; UniProt 1–403 Author chain DG; PDBConstruct 1–403; UniProt 1–403 Author chain DH; PDBConstruct 1–403; UniProt 1–403 Author chain DI; PDBConstruct 1–403; UniProt 1–403 Author chain DJ; PDBConstruct 1–403; UniProt 1–403 Author chain DK; PDBConstruct 1–403; UniProt 1–403 Author chain DL; PDBConstruct 1–403; UniProt 1–403 Author chain DM; PDBConstruct 1–403; UniProt 1–403 Author chain DN; PDBConstruct 1–403; UniProt 1–403 Author chain DO; PDBConstruct 1–403; UniProt 1–403 Author chain DP; PDBConstruct 1–403; UniProt 1–403 Author chain DQ; PDBConstruct 1–403; UniProt 1–403 Author chain DR; PDBConstruct 1–403; UniProt 1–403 Author chain DS; PDBConstruct 1–403; UniProt 1–403 Author chain DT; PDBConstruct 1–403; UniProt 1–403 Author chain DU; PDBConstruct 1–403; UniProt 1–403 Author chain DV; PDBConstruct 1–403; UniProt 1–403 Author chain DW; PDBConstruct 1–403; UniProt 1–403 Author chain DX; PDBConstruct 1–403; UniProt 1–403 Author chain DY; PDBConstruct 1–403; UniProt 1–403 Author chain DZ; PDBConstruct 1–403; UniProt 1–403 Author chain EA; PDBConstruct 1–403; UniProt 1–403 Author chain EB; PDBConstruct 1–403; UniProt 1–403 Author chain EC; PDBConstruct 1–403; UniProt 1–403 Author chain ED; PDBConstruct 1–403; UniProt 1–403 Author chain EE; PDBConstruct 1–403; UniProt 1–403 Author chain EF; PDBConstruct 1–403; UniProt 1–403 Author chain EG; PDBConstruct 1–403; UniProt 1–403

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 × 219 PDB declaration: 219-meric(219) Consistent with protein copy count Chain CE; UniProt 1–264 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 33 (P0A1J1) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar M-ring protein × 57 (P15928) FlgB-Dc loop × 5 FliE helix 1 × 6 Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.90 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 9
Chains and sequence ranges Author chain CE; PDBConstruct 1–264; UniProt 1–264

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 × 219 PDB declaration: 219-meric(219) Consistent with protein copy count Chain CA; UniProt 1–89 Chain CB; UniProt 1–89 Chain CC; UniProt 1–89 Chain CD; UniProt 1–89 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 33 (P0A1J1) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar M-ring protein × 57 (P15928) FlgB-Dc loop × 5 FliE helix 1 × 6 Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.90 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 10
Chains and sequence ranges Author chain CA; PDBConstruct 1–89; UniProt 1–89 Author chain CB; PDBConstruct 1–89; UniProt 1–89 Author chain CC; PDBConstruct 1–89; UniProt 1–89 Author chain CD; PDBConstruct 1–89; UniProt 1–89

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 × 219 PDB declaration: 219-meric(219) Consistent with protein copy count Chain CF; UniProt 1–245 Chain w; UniProt 1–245 Chain x; UniProt 1–245 Chain y; UniProt 1–245 Chain z; UniProt 1–245 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 33 (P0A1J1) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar M-ring protein × 57 (P15928) FlgB-Dc loop × 5 FliE helix 1 × 6 Flagellar L-ring protein × 26 (P0A1N8) Flagellar P-ring protein × 26 (P15930) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.90 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 11
Chains and sequence ranges Author chain CF; PDBConstruct 1–245; UniProt 1–245 Author chain w; PDBConstruct 1–245; UniProt 1–245 Author chain x; PDBConstruct 1–245; UniProt 1–245 Author chain y; PDBConstruct 1–245; UniProt 1–245 Author chain z; PDBConstruct 1–245; UniProt 1–245

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 × 219 PDB declaration: 219-meric(219) Consistent with protein copy count Chain AA; UniProt 1–232 Chain AB; UniProt 1–232 Chain AC; UniProt 1–232 Chain AD; UniProt 1–232 Chain AE; UniProt 1–232 Chain AF; UniProt 1–232 Chain AG; UniProt 1–232 Chain AH; UniProt 1–232 Chain AI; UniProt 1–232 Chain AJ; UniProt 1–232 Chain AK; UniProt 1–232 Chain AL; UniProt 1–232 Chain AM; UniProt 1–232 Chain AN; UniProt 1–232 Chain AO; UniProt 1–232 Chain AP; UniProt 1–232 Chain AQ; UniProt 1–232 Chain AR; UniProt 1–232 Chain AS; UniProt 1–232 Chain AT; UniProt 1–232 Chain AU; UniProt 1–232 Chain AV; UniProt 1–232 Chain AW; UniProt 1–232 Chain AX; UniProt 1–232 Chain AY; UniProt 1–232 Chain AZ; UniProt 1–232 Non-standard monomer:Yes (specific site not provided by mmCIF) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 33 (P0A1J1) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar M-ring protein × 57 (P15928) FlgB-Dc loop × 5 FliE helix 1 × 6 Flagellar P-ring protein × 26 (P15930) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.90 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 15
Chains and sequence ranges Author chain AA; PDBConstruct 1–232; UniProt 1–232 Author chain AB; PDBConstruct 1–232; UniProt 1–232 Author chain AC; PDBConstruct 1–232; UniProt 1–232 Author chain AD; PDBConstruct 1–232; UniProt 1–232 Author chain AE; PDBConstruct 1–232; UniProt 1–232 Author chain AF; PDBConstruct 1–232; UniProt 1–232 Author chain AG; PDBConstruct 1–232; UniProt 1–232 Author chain AH; PDBConstruct 1–232; UniProt 1–232 Author chain AI; PDBConstruct 1–232; UniProt 1–232 Author chain AJ; PDBConstruct 1–232; UniProt 1–232 Author chain AK; PDBConstruct 1–232; UniProt 1–232 Author chain AL; PDBConstruct 1–232; UniProt 1–232 Author chain AM; PDBConstruct 1–232; UniProt 1–232 Author chain AN; PDBConstruct 1–232; UniProt 1–232 Author chain AO; PDBConstruct 1–232; UniProt 1–232 Author chain AP; PDBConstruct 1–232; UniProt 1–232 Author chain AQ; PDBConstruct 1–232; UniProt 1–232 Author chain AR; PDBConstruct 1–232; UniProt 1–232 Author chain AS; PDBConstruct 1–232; UniProt 1–232 Author chain AT; PDBConstruct 1–232; UniProt 1–232 Author chain AU; PDBConstruct 1–232; UniProt 1–232 Author chain AV; PDBConstruct 1–232; UniProt 1–232 Author chain AW; PDBConstruct 1–232; UniProt 1–232 Author chain AX; PDBConstruct 1–232; UniProt 1–232 Author chain AY; PDBConstruct 1–232; UniProt 1–232 Author chain AZ; 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 × 219 PDB declaration: 219-meric(219) Consistent with protein copy count Chain BA; UniProt 1–365 Chain BB; UniProt 1–365 Chain BC; UniProt 1–365 Chain BD; UniProt 1–365 Chain BE; UniProt 1–365 Chain BF; UniProt 1–365 Chain BG; UniProt 1–365 Chain BH; UniProt 1–365 Chain BI; UniProt 1–365 Chain BJ; UniProt 1–365 Chain BK; UniProt 1–365 Chain BL; UniProt 1–365 Chain BM; UniProt 1–365 Chain BN; UniProt 1–365 Chain BO; UniProt 1–365 Chain BP; UniProt 1–365 Chain BQ; UniProt 1–365 Chain BR; UniProt 1–365 Chain BS; UniProt 1–365 Chain BT; UniProt 1–365 Chain BU; UniProt 1–365 Chain BV; UniProt 1–365 Chain BW; UniProt 1–365 Chain BX; UniProt 1–365 Chain BY; UniProt 1–365 Chain BZ; UniProt 1–365 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 33 (P0A1J1) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar M-ring protein × 57 (P15928) FlgB-Dc loop × 5 FliE helix 1 × 6 Flagellar L-ring protein × 26 (P0A1N8) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.90 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 16
Chains and sequence ranges Author chain BA; PDBConstruct 1–365; UniProt 1–365 Author chain BB; PDBConstruct 1–365; UniProt 1–365 Author chain BC; PDBConstruct 1–365; UniProt 1–365 Author chain BD; PDBConstruct 1–365; UniProt 1–365 Author chain BE; PDBConstruct 1–365; UniProt 1–365 Author chain BF; PDBConstruct 1–365; UniProt 1–365 Author chain BG; PDBConstruct 1–365; UniProt 1–365 Author chain BH; PDBConstruct 1–365; UniProt 1–365 Author chain BI; PDBConstruct 1–365; UniProt 1–365 Author chain BJ; PDBConstruct 1–365; UniProt 1–365 Author chain BK; PDBConstruct 1–365; UniProt 1–365 Author chain BL; PDBConstruct 1–365; UniProt 1–365 Author chain BM; PDBConstruct 1–365; UniProt 1–365 Author chain BN; PDBConstruct 1–365; UniProt 1–365 Author chain BO; PDBConstruct 1–365; UniProt 1–365 Author chain BP; PDBConstruct 1–365; UniProt 1–365 Author chain BQ; PDBConstruct 1–365; UniProt 1–365 Author chain BR; PDBConstruct 1–365; UniProt 1–365 Author chain BS; PDBConstruct 1–365; UniProt 1–365 Author chain BT; PDBConstruct 1–365; UniProt 1–365 Author chain BU; PDBConstruct 1–365; UniProt 1–365 Author chain BV; PDBConstruct 1–365; UniProt 1–365 Author chain BW; PDBConstruct 1–365; UniProt 1–365 Author chain BX; PDBConstruct 1–365; UniProt 1–365 Author chain BY; PDBConstruct 1–365; UniProt 1–365 Author chain BZ; PDBConstruct 1–365; UniProt 1–365

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 7cgo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7cgo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7cgo
Deposition date deposition_date2020-07-01
Structure title titleCryo-EM structure of the flagellar motor-hook complex from Salmonella
Keywords keywordsFlagella, Hook-basal body, 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_electron137.40
Forward intensity I(0) i0334285000000.00
Molecular weight molecular_weight4779500.0 kDa
Excluded volume excluded_volume5915500 ų
Envelope volume envelope_volume10567000 ų
Hydration-shell volume shell_volume629250 ų
Envelope diameter envelope_diameter514.8
Shell Rg shell_rg130.10
Envelope Rg envelope_rg141.10
Shape Rg shape_rg137.40
Total Rg total_rg137.20
Total atoms total_atoms335722
Residues n_residues45082
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 dmax397.7
Rg (real space) rg_real129.60
Rg uncertainty (real space) rg_real_error2.07
I(0) (real space) i0_real3.2080e+11
I(0) uncertainty (real space) i0_real_error7.8560e+09
Rg (reciprocal space) rg_reciprocal122.40
I(0) (reciprocal space) i0_reciprocal318500000000.0000
Solution quality estimate total_estimate0.8946
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary144.6
Skewness Skewness skewness0.507
Kurtosis Kurtosis kurtosis-0.187
Angular range angular_range— – 0.0550 −1
Current regularization parameter α current_alpha0.9484
Highest regularization parameter α highest_alpha25410000000.0000
Real-space data points n_real_points12
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.009; Oscil: 0.931; Stabil: 0.979; Sysdev: 1.000; Positv: 1.000; Valcen: 0.899; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

8. Citations (1)

9. Files and Curves (10)