6vq8

Mammalian V-ATPase from rat brain - composite model of rotational state 3 bound to ADP and SidK (built from focused refinement models)

Method: ELECTRON MICROSCOPY Dmax: 214.9 Å Quality: GOOD

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

ATPase H+-transporting V1 subunit A

OrganismNot specified

UniProt D4A133

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain A; UniProt 1–617 Chain B; UniProt 1–617 Chain C; UniProt 1–617 Not recorded V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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 D4A133_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–617; UniProt 1–617 Author chain B; PDBConstruct 1–617; UniProt 1–617 Author chain C; PDBConstruct 1–617; UniProt 1–617

V-type proton ATPase subunit B, brain isoform

OrganismNot specified

UniProt P62815

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain D; UniProt 1–511 Chain E; UniProt 1–511 Chain F; UniProt 1–511 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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 VATB2_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–511; UniProt 1–511 Author chain E; PDBConstruct 1–511; UniProt 1–511 Author chain F; PDBConstruct 1–511; UniProt 1–511

V-type proton ATPase subunit C 1

OrganismNot specified

UniProt Q5FVI6

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain G; UniProt 1–382 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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 VATC1_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–382; UniProt 1–382

ATPase H+-transporting V1 subunit D

OrganismNot specified

UniProt Q6P503

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain H; UniProt 1–247 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6P503_RAT
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–247; UniProt 1–247

V-type proton ATPase subunit E 1

OrganismNot specified

UniProt Q6PCU2

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain I; UniProt 1–226 Chain J; UniProt 1–226 Chain K; UniProt 1–226 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATE1_RAT
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–226; UniProt 1–226 Author chain J; PDBConstruct 1–226; UniProt 1–226 Author chain K; PDBConstruct 1–226; UniProt 1–226

V-type proton ATPase subunit F

OrganismNot specified

UniProt P50408

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain L; UniProt 1–119 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATF_RAT
Isoform
PDB entities 6
Chains and sequence ranges Author chain L; PDBConstruct 1–119; UniProt 1–119

V-type proton ATPase subunit G

OrganismNot specified

UniProt Q8R2H0

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain M; UniProt 1–118 Chain N; UniProt 1–118 Chain O; UniProt 1–118 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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 Q8R2H0_RAT
Isoform
PDB entities 7
Chains and sequence ranges Author chain M; PDBConstruct 1–118; UniProt 1–118 Author chain N; PDBConstruct 1–118; UniProt 1–118 Author chain O; PDBConstruct 1–118; UniProt 1–118

Effector protein SidK

Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)

UniProt Q5ZWW6

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain Q; UniProt 1–278 Chain R; UniProt 1–278 Chain S; UniProt 1–278 Fragment:N-terminal fragment with 3x FLAG tag ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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.

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

View Construct and Data Evidence
UniProt name Q5ZWW6_LEGPH
Isoform
PDB entities 8
Chains and sequence ranges Author chain Q; PDBConstruct 2–279; UniProt 1–278 Author chain R; PDBConstruct 2–279; UniProt 1–278 Author chain S; PDBConstruct 2–279; UniProt 1–278

V-type proton ATPase 116 kDa subunit a isoform 1

OrganismNot specified

UniProt P25286

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain a; UniProt 1–838 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPP1_RAT
Isoform
PDB entities 9
Chains and sequence ranges Author chain a; PDBConstruct 1–838; UniProt 1–838

ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a

OrganismNot specified

UniProt B0K022

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain b; UniProt 1–205 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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 B0K022_RAT
Isoform
PDB entities 10
Chains and sequence ranges Author chain b; PDBConstruct 1–205; UniProt 1–205

V-type proton ATPase subunit S1

OrganismNot specified

UniProt O54715

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain c; UniProt 1–463 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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 VAS1_RAT
Isoform
PDB entities 11
Chains and sequence ranges Author chain c; PDBConstruct 1–463; UniProt 1–463

V-type proton ATPase subunit

OrganismNot specified

UniProt Q5M7T6

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain d; UniProt 1–351 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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 Q5M7T6_RAT
Isoform
PDB entities 12
Chains and sequence ranges Author chain d; PDBConstruct 1–351; UniProt 1–351

V-type proton ATPase subunit e 2

OrganismNot specified

UniProt Q5EB76

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain e; UniProt 1–81 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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 VA0E2_RAT
Isoform
PDB entities 13
Chains and sequence ranges Author chain e; PDBConstruct 1–81; UniProt 1–81

Ribonuclease K

OrganismNot specified

UniProt D3ZIM6

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain f; UniProt 1–98 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D3ZIM6_RAT
Isoform
PDB entities 14
Chains and sequence ranges Author chain f; PDBConstruct 1–98; UniProt 1–98

V-type proton ATPase 16 kDa proteolipid subunit

OrganismNot specified

UniProt P63081

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain g; UniProt 1–155 Chain h; UniProt 1–155 Chain i; UniProt 1–155 Chain j; UniProt 1–155 Chain k; UniProt 1–155 Chain l; UniProt 1–155 Chain m; UniProt 1–155 Chain n; UniProt 1–155 Chain o; UniProt 1–155 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) Renin receptor × 1 (Q6AXS4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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 VATL_RAT
Isoform
PDB entities 15
Chains and sequence ranges Author chain g; PDBConstruct 1–155; UniProt 1–155 Author chain h; PDBConstruct 1–155; UniProt 1–155 Author chain i; PDBConstruct 1–155; UniProt 1–155 Author chain j; PDBConstruct 1–155; UniProt 1–155 Author chain k; PDBConstruct 1–155; UniProt 1–155 Author chain l; PDBConstruct 1–155; UniProt 1–155 Author chain m; PDBConstruct 1–155; UniProt 1–155 Author chain n; PDBConstruct 1–155; UniProt 1–155 Author chain o; PDBConstruct 1–155; UniProt 1–155

Renin receptor

OrganismNot specified

UniProt Q6AXS4

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain p; UniProt 1–350 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE 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 RENR_RAT
Isoform
PDB entities 16
Chains and sequence ranges Author chain p; PDBConstruct 1–350; UniProt 1–350

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 6vq8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6vq8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6vq8
Deposition date deposition_date2020-02-04
Structure title titleMammalian V-ATPase from rat brain - composite model of rotational state 3 bound to ADP and SidK (built from focused refinement models)
Keywords keywordsmembrane protein complex, rotary atpase, PROTON TRANSPORT; PROTON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier79.71
Radius of gyration Rg (electron density) rg_electron80.14
Forward intensity I(0) i010338200000.00
Molecular weight molecular_weight862450.0 kDa
Excluded volume excluded_volume1078100 ų
Envelope volume envelope_volume1785100 ų
Hydration-shell volume shell_volume185550 ų
Envelope diameter envelope_diameter264.9
Shell Rg shell_rg78.74
Envelope Rg envelope_rg77.37
Shape Rg shape_rg80.17
Total Rg total_rg80.01
Total atoms total_atoms60714
Residues n_residues8451
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 dmax214.9
Rg (real space) rg_real77.58
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real1.0030e+10
I(0) uncertainty (real space) i0_real_error1.9570e+08
Rg (reciprocal space) rg_reciprocal78.46
I(0) (reciprocal space) i0_reciprocal10300000000.0000
Solution quality estimate total_estimate0.8908
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.2
Skewness Skewness skewness0.318
Kurtosis Kurtosis kurtosis-0.759
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.6806
Highest regularization parameter α highest_alpha2038000000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.987; Stabil: 0.988; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (17)

7. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

Domain ID domain_id6vq8A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6vq8A03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain
Domain ID domain_id6vq8B02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6vq8B03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain
Domain ID domain_id6vq8C02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6vq8C03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain
Domain ID domain_id6vq8D00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily12240
Domain ID domain_id6vq8E00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily12240
Domain ID domain_id6vq8F00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily12240
Domain ID domain_id6vq8G02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1460 — subunit c (vma5p) of the yeast v-atpase, domain 2
Homologous superfamily homologous superfamily10 — subunit c (vma5p) of the yeast v-atpase, domain 2
Domain ID domain_id6vq8G03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily100
Domain ID domain_id6vq8H01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily3240
Domain ID domain_id6vq8I01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily30 — ATP synthase, E subunit, C-terminal
Domain ID domain_id6vq8J01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily30 — ATP synthase, E subunit, C-terminal
Domain ID domain_id6vq8K01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily30 — ATP synthase, E subunit, C-terminal
Domain ID domain_id6vq8L00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10580 — ATPase, V1 complex, subunit F

8. Citations (1)

9. Files and Curves (10)