6xbw

Cryo-EM structure of V-ATPase from bovine brain, state 1

Method: ELECTRON MICROSCOPY Dmax: 218.3 Å Quality: GOOD

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

V-type proton ATPase catalytic subunit A

OrganismNot specified

UniProt P31404

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 × 32 PDB declaration: 32-meric(32) 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 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

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

View Construct and Data Evidence
UniProt name VATA_BOVIN
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 P31408

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain D; UniProt 1–511 Chain E; UniProt 1–511 Chain F; UniProt 1–511 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

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

View Construct and Data Evidence
UniProt name VATB2_BOVIN
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 P21282

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain G; UniProt 1–382 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATC1_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–382; UniProt 1–382

V-type proton ATPase subunit D

OrganismNot specified

UniProt A0A3Q1M4W9

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain H; UniProt 1–247 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

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

View Construct and Data Evidence
UniProt name A0A3Q1M4W9_BOVIN
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 P11019

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain I; UniProt 1–226 Chain J; UniProt 1–226 Chain K; UniProt 1–226 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

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

View Construct and Data Evidence
UniProt name VATE1_BOVIN
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 Q28029

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain L; UniProt 1–119 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATF_BOVIN
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 Q0VCV6

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain M; UniProt 1–118 Chain N; UniProt 1–118 Chain O; UniProt 1–118 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

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

View Construct and Data Evidence
UniProt name Q0VCV6_BOVIN
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

V-type proton ATPase subunit H

OrganismNot specified

UniProt F1MZL6

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain P; UniProt 1–465 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F1MZL6_BOVIN
Isoform
PDB entities 8
Chains and sequence ranges Author chain P; PDBConstruct 1–465; UniProt 1–465

V-type proton ATPase subunit a

OrganismNot specified

UniProt F1MJV0

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain a; UniProt 1–838 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F1MJV0_BOVIN
Isoform
PDB entities 9
Chains and sequence ranges Author chain a; PDBConstruct 1–838; UniProt 1–838

V-type proton ATPase 21 kDa proteolipid subunit

OrganismNot specified

UniProt Q2TA24

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain b; UniProt 1–205 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATO_BOVIN
Isoform
PDB entities 10
Chains and sequence ranges Author chain b; PDBConstruct 1–205; UniProt 1–205

V-type proton ATPase subunit d 1

OrganismNot specified

UniProt P61420

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain d; UniProt 1–351 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0D1_BOVIN
Isoform
PDB entities 11
Chains and sequence ranges Author chain d; PDBConstruct 1–351; UniProt 1–351

V-type proton ATPase subunit e 2

OrganismNot specified

UniProt Q2KIB5

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain e; UniProt 1–81 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0E2_BOVIN
Isoform
PDB entities 12
Chains and sequence ranges Author chain e; PDBConstruct 1–81; UniProt 1–81

V-type proton ATPase subunit S1

OrganismNot specified

UniProt P40682

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain s; UniProt 1–468 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VAS1_BOVIN
Isoform
PDB entities 13
Chains and sequence ranges Author chain s; PDBConstruct 1–468; UniProt 1–468

Renin receptor

OrganismNot specified

UniProt P81134

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain r; UniProt 1–351 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RENR_BOVIN
Isoform
PDB entities 14
Chains and sequence ranges Author chain r; PDBConstruct 1–351; UniProt 1–351

V-type proton ATPase 16 kDa proteolipid subunit

OrganismNot specified

UniProt P23956

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain c; UniProt 1–155 Chain g; 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 Chain p; UniProt 1–155 Chain q; UniProt 1–155 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) Ribonuclease kappa × 1 (Q3ZC23) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL_BOVIN
Isoform
PDB entities 15
Chains and sequence ranges Author chain c; PDBConstruct 1–155; UniProt 1–155 Author chain g; 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 Author chain p; PDBConstruct 1–155; UniProt 1–155 Author chain q; PDBConstruct 1–155; UniProt 1–155

Ribonuclease kappa

OrganismNot specified

UniProt Q3ZC23

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain f; UniProt 1–98 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit C 1 × 1 (P21282) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit F × 1 (Q28029) V-type proton ATPase subunit G × 3 (Q0VCV6) V-type proton ATPase subunit H × 1 (F1MZL6) V-type proton ATPase subunit a × 1 (F1MJV0) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q2TA24) V-type proton ATPase subunit d 1 × 1 (P61420) V-type proton ATPase subunit e 2 × 1 (Q2KIB5) V-type proton ATPase subunit S1 × 1 (P40682) Renin receptor × 1 (P81134) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P23956) MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 OLA OLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNK_BOVIN
Isoform
PDB entities 16
Chains and sequence ranges Author chain f; PDBConstruct 1–98; UniProt 1–98

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 6xbw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6xbw
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6xbw
Deposition date deposition_date2020-06-07
Structure title titleCryo-EM structure of V-ATPase from bovine brain, state 1
Keywords keywordsPROTON TRANSPORT; PROTON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier80.94
Radius of gyration Rg (electron density) rg_electron81.87
Forward intensity I(0) i010423400000.00
Molecular weight molecular_weight897200.0 kDa
Excluded volume excluded_volume1134700 ų
Envelope volume envelope_volume1804900 ų
Hydration-shell volume shell_volume187520 ų
Envelope diameter envelope_diameter282.4
Shell Rg shell_rg79.20
Envelope Rg envelope_rg77.85
Shape Rg shape_rg81.88
Total Rg total_rg81.81
Total atoms total_atoms63090
Residues n_residues8186
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 dmax218.3
Rg (real space) rg_real78.26
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real1.0150e+10
I(0) uncertainty (real space) i0_real_error1.9860e+08
Rg (reciprocal space) rg_reciprocal79.34
I(0) (reciprocal space) i0_reciprocal10380000000.0000
Solution quality estimate total_estimate0.8808
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary80.4
Skewness Skewness skewness0.350
Kurtosis Kurtosis kurtosis-0.657
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.1561
Highest regularization parameter α highest_alpha1416000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.960; Stabil: 0.984; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.006

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (21)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6xbwH01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily3240
Domain ID domain_id6xbwI01
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_id6xbwJ01
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_id6xbwK01
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

8. Citations (1)

9. Files and Curves (10)