7fda

CryoEM Structure of Reconstituted V-ATPase, state1

Method: ELECTRON MICROSCOPY Dmax: 281.4 Å Quality: GOOD

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

V-type proton ATPase subunit B

OrganismNot specified

UniProt P16140

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain B; UniProt 1–517 Chain D; UniProt 1–517 Chain F; UniProt 1–517 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATB_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–517; UniProt 1–517 Author chain D; PDBConstruct 1–517; UniProt 1–517 Author chain F; PDBConstruct 1–517; UniProt 1–517

V-type proton ATPase subunit E

OrganismNot specified

UniProt P22203

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain G; UniProt 1–233 Chain I; UniProt 1–233 Chain K; UniProt 1–233 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

21 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATE_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–233; UniProt 1–233 Author chain I; PDBConstruct 1–233; UniProt 1–233 Author chain K; PDBConstruct 1–233; UniProt 1–233

V-type proton ATPase subunit D

OrganismNot specified

UniProt P32610

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain M; UniProt 1–256 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATD_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain M; PDBConstruct 1–256; UniProt 1–256

V-type proton ATPase subunit F

OrganismNot specified

UniProt P39111

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain N; UniProt 1–118 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit C × 1 (P31412) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATF_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain N; PDBConstruct 1–118; UniProt 1–118

V-type proton ATPase subunit C

Saccharomyces cerevisiae S288C

UniProt P31412

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain O; UniProt 1–392 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

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

View Construct and Data Evidence
UniProt name VATC_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain O; PDBConstruct 1–392; UniProt 1–392

Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT)

Homo sapiens

UniProt P41807

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain P; UniProt 1–359 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

24 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATH_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain P; PDBConstruct 1–359; UniProt 1–359

Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT)

Homo sapiens

UniProt Q9UI12

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain P; UniProt 356–465 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name VATH_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain P; PDBConstruct 360–469; UniProt 356–465

Yeast Vacuolar ATPase a subunit

OrganismNot specified

UniProt P32563

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain Q; UniProt 1–840 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPH1_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain Q; PDBConstruct 1–840; UniProt 1–840

V-type proton ATPase subunit d

OrganismNot specified

UniProt P32366

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain S; UniProt 1–345 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) Yeast Vacuolar ATPase a subunit × 1 (P32563) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0D_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain S; PDBConstruct 1–345; UniProt 1–345

;V-type proton ATPase subunit c'' ;

OrganismNot specified

UniProt P23968

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain T; UniProt 1–213 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATO_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain T; PDBConstruct 1–213; UniProt 1–213

;V-type proton ATPase subunit c' ;

OrganismNot specified

UniProt P32842

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain U; UniProt 1–164 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL2_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain U; PDBConstruct 1–164; UniProt 1–164

V-type proton ATPase subunit c

OrganismNot specified

UniProt P25515

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain V; UniProt 1–160 Chain W; UniProt 1–160 Chain X; UniProt 1–160 Chain Y; UniProt 1–160 Chain Z; UniProt 1–160 Chain a; UniProt 1–160 Chain b; UniProt 1–160 Chain c; UniProt 1–160 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL1_YEAST
Isoform
PDB entities 13
Chains and sequence ranges Author chain V; PDBConstruct 1–160; UniProt 1–160 Author chain W; PDBConstruct 1–160; UniProt 1–160 Author chain X; PDBConstruct 1–160; UniProt 1–160 Author chain Y; PDBConstruct 1–160; UniProt 1–160 Author chain Z; PDBConstruct 1–160; UniProt 1–160 Author chain a; PDBConstruct 1–160; UniProt 1–160 Author chain b; PDBConstruct 1–160; UniProt 1–160 Author chain c; PDBConstruct 1–160; UniProt 1–160

V-type proton ATPase subunit e

OrganismNot specified

UniProt Q3E7B6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain d; UniProt 1–73 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V0 assembly protein 1 × 1 (P53262) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0E_YEAST
Isoform
PDB entities 14
Chains and sequence ranges Author chain d; PDBConstruct 1–73; UniProt 1–73

V0 assembly protein 1

OrganismNot specified

UniProt P53262

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain e; UniProt 1–265 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) Yeast Vacuolar ATPase f subunit × 1 (P0C5R9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VOA1_YEAST
Isoform
PDB entities 15
Chains and sequence ranges Author chain e; PDBConstruct 1–265; UniProt 1–265

Yeast Vacuolar ATPase f subunit

OrganismNot specified

UniProt P0C5R9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain f; UniProt 1–85 Not recorded Yeast Vacuolar ATPase A subunit × 3 V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Fusion of yeast V-type proton ATPase subunit H(NT) and human V-type proton ATPase subunit H(CT) × 1 (P41807,Q9UI12) Yeast Vacuolar ATPase a subunit × 1 (P32563) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V0 assembly protein 1 × 1 (P53262) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YP17B_YEAST
Isoform
PDB entities 16
Chains and sequence ranges Author chain f; PDBConstruct 1–85; UniProt 1–85

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 7fda

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7fda
Deposition date deposition_date2021-07-16
Structure title titleCryoEM Structure of Reconstituted V-ATPase, state1
Keywords keywordsATPase, proton pump, rotary motor enzyme, membrane protein, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier81.20
Radius of gyration Rg (electron density) rg_electron82.07
Forward intensity I(0) i010737500000.00
Molecular weight molecular_weight916190.0 kDa
Excluded volume excluded_volume1161000 ų
Envelope volume envelope_volume1925400 ų
Hydration-shell volume shell_volume196560 ų
Envelope diameter envelope_diameter270.3
Shell Rg shell_rg81.18
Envelope Rg envelope_rg78.26
Shape Rg shape_rg82.05
Total Rg total_rg82.16
Total atoms total_atoms64497
Residues n_residues8295
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 dmax281.4
Rg (real space) rg_real85.02
Rg uncertainty (real space) rg_real_error1.62
I(0) (real space) i0_real1.0740e+10
I(0) uncertainty (real space) i0_real_error2.3350e+08
Rg (reciprocal space) rg_reciprocal80.14
I(0) (reciprocal space) i0_reciprocal10700000000.0000
Solution quality estimate total_estimate0.8645
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary74.1
Skewness Skewness skewness0.476
Kurtosis Kurtosis kurtosis-0.376
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha1.4220
Highest regularization parameter α highest_alpha1709000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.846; Stabil: 0.873; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.097

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

8. Citations (1)

9. Files and Curves (10)