9moy

Reconstituted yeast V-ATPase bound to Rtc5p

Method: ELECTRON MICROSCOPY Dmax: 210.4 Å Quality: REASONABLE

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

H(+)-transporting two-sector ATPase

OrganismNot specified

UniProt B3LH69

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 C; UniProt 1–617 Chain E; UniProt 1–617 Not recorded V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name B3LH69_YEAS1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–617; UniProt 1–617 Author chain C; PDBConstruct 1–617; UniProt 1–617 Author chain E; PDBConstruct 1–617; UniProt 1–617

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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain G; UniProt 1–233 Chain I; UniProt 1–233 Chain K; UniProt 1–233 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 2
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 G

OrganismNot specified

UniProt P48836

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 1–114 Chain J; UniProt 1–114 Chain L; UniProt 1–114 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 Å

Other States of the Same Protein in the Database

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

20 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATG_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 1–114; UniProt 1–114 Author chain J; PDBConstruct 1–114; UniProt 1–114 Author chain L; PDBConstruct 1–114; UniProt 1–114

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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain M; UniProt 1–256 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 4
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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain N; UniProt 1–118 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 5
Chains and sequence ranges Author chain N; PDBConstruct 1–118; UniProt 1–118

V-type proton ATPase subunit C

OrganismNot specified

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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain O; UniProt 1–392 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 6
Chains and sequence ranges Author chain O; PDBConstruct 1–392; UniProt 1–392

Restriction of telomere capping protein 5

Saccharomyces cerevisiae

UniProt B3LJG1

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 1–567 Mutation:N-terminal 6xHis-tag H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 RTC5_YEAS1
Isoform
PDB entities 7
Chains and sequence ranges Author chain R; PDBConstruct 1–567; UniProt 1–567

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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain S; UniProt 1–345 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) ;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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 8
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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain T; UniProt 1–213 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 9
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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain U; UniProt 1–164 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 10
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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) 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 H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 11
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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain d; UniProt 1–73 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 12
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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain e; UniProt 1–265 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 13
Chains and sequence ranges Author chain e; PDBConstruct 1–265; UniProt 1–265

Yeast V-ATPase subunit f

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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain f; UniProt 1–85 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 14
Chains and sequence ranges Author chain f; PDBConstruct 1–85; UniProt 1–85

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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain B; UniProt 1–517 Chain D; UniProt 1–517 Chain F; UniProt 1–517 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 15
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 H

OrganismNot specified

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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain P; UniProt 1–478 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 16
Chains and sequence ranges Author chain P; PDBConstruct 1–478; UniProt 1–478

V-type proton ATPase subunit a, vacuolar isoform

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 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain Q; UniProt 1–840 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit C × 1 (P31412) Restriction of telomere capping protein 5 × 1 (B3LJG1) 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 V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Leica EM GP2 Resolution 3.60 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 17
Chains and sequence ranges Author chain Q; PDBConstruct 1–840; UniProt 1–840

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 9moy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9moy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9moy
Deposition date deposition_date2024-12-28
Structure title titleReconstituted yeast V-ATPase bound to Rtc5p
Keywords keywordsVacuolar ATPase, proton pump, Rtc5p, membrane protein, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier79.42
Radius of gyration Rg (electron density) rg_electron80.15
Forward intensity I(0) i012299100000.00
Molecular weight molecular_weight979000.0 kDa
Excluded volume excluded_volume1239900 ų
Envelope volume envelope_volume2001700 ų
Hydration-shell volume shell_volume207640 ų
Envelope diameter envelope_diameter269.9
Shell Rg shell_rg81.22
Envelope Rg envelope_rg76.67
Shape Rg shape_rg80.12
Total Rg total_rg80.25
Total atoms total_atoms138815
Residues n_residues8847
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 dmax210.4
Rg (real space) rg_real76.31
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.1830e+10
I(0) uncertainty (real space) i0_real_error2.0540e+08
Rg (reciprocal space) rg_reciprocal78.79
I(0) (reciprocal space) i0_reciprocal12280000000.0000
Solution quality estimate total_estimate0.6865
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary84.2
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.576
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.4301
Highest regularization parameter α highest_alpha1453000000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.992; Stabil: 0.982; Sysdev: 0.002; Positv: 1.000; Valcen: 0.994; Smooth: 0.014

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

8. Citations (1)

9. Files and Curves (10)