9cf8

Cryo-EM structure of human kidney V-ATPase state 1

Method: ELECTRON MICROSCOPY Dmax: 231.4 Å Quality: GOOD

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

V-type proton ATPase 21 kDa proteolipid subunit

OrganismNot specified

UniProt Q99437

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain 0; UniProt 1–205 Not recorded V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 VATO_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain 0; PDBConstruct 1–205; UniProt 1–205

V-type proton ATPase 16 kDa proteolipid subunit

OrganismNot specified

UniProt P27449

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain 1; UniProt 1–155 Chain 2; UniProt 1–155 Chain 3; UniProt 1–155 Chain 4; UniProt 1–155 Chain 5; UniProt 1–155 Chain 6; UniProt 1–155 Chain 7; UniProt 1–155 Chain 8; UniProt 1–155 Chain 9; UniProt 1–155 Not recorded V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 VATL_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain 1; PDBConstruct 1–155; UniProt 1–155 Author chain 2; PDBConstruct 1–155; UniProt 1–155 Author chain 3; PDBConstruct 1–155; UniProt 1–155 Author chain 4; PDBConstruct 1–155; UniProt 1–155 Author chain 5; PDBConstruct 1–155; UniProt 1–155 Author chain 6; PDBConstruct 1–155; UniProt 1–155 Author chain 7; PDBConstruct 1–155; UniProt 1–155 Author chain 8; PDBConstruct 1–155; UniProt 1–155 Author chain 9; PDBConstruct 1–155; UniProt 1–155

V-type proton ATPase catalytic subunit A

OrganismNot specified

UniProt P38606

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 × 30 PDB declaration: 30-meric(30) 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 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 VATA_HUMAN
Isoform
PDB entities 3
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 P21281

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 × 30 PDB declaration: 30-meric(30) 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 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 VATB2_HUMAN
Isoform
PDB entities 4
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 D

OrganismNot specified

UniProt Q9Y5K8

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain G; UniProt 1–247 Not recorded V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 VATD_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–247; UniProt 1–247

V-type proton ATPase subunit E 1

OrganismNot specified

UniProt P36543

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain H; UniProt 1–226 Chain I; UniProt 1–226 Chain J; UniProt 1–226 Not recorded V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 VATE1_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain H; PDBConstruct 1–226; UniProt 1–226 Author chain I; PDBConstruct 1–226; UniProt 1–226 Author chain J; PDBConstruct 1–226; UniProt 1–226

V-type proton ATPase subunit G 1

OrganismNot specified

UniProt O75348

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain K; UniProt 1–118 Chain L; UniProt 1–118 Chain M; UniProt 1–118 Not recorded V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 VATG1_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–118; UniProt 1–118 Author chain L; PDBConstruct 1–118; UniProt 1–118 Author chain M; PDBConstruct 1–118; UniProt 1–118

V-type proton ATPase subunit F

OrganismNot specified

UniProt Q16864

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain N; UniProt 1–119 Not recorded V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 VATF_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain N; PDBConstruct 1–119; UniProt 1–119

V-type proton ATPase subunit d 1

OrganismNot specified

UniProt P61421

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain Q; UniProt 1–351 Not recorded V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 VA0D1_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain Q; PDBConstruct 1–351; UniProt 1–351

V-type proton ATPase 116 kDa subunit a isoform 1

OrganismNot specified

UniProt Q93050

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain R; UniProt 1–837 Not recorded V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPP1_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain R; PDBConstruct 1–837; UniProt 1–837

V-type proton ATPase subunit e 1

OrganismNot specified

UniProt O15342

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain S; UniProt 1–81 Not recorded V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 VA0E1_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain S; PDBConstruct 1–81; UniProt 1–81

Ribonuclease kappa

OrganismNot specified

UniProt Q6P5S7

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain T; UniProt 1–137 Not recorded V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit e 1 × 1 (O15342) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 RNK_HUMAN
Isoform
PDB entities 12
Chains and sequence ranges Author chain T; PDBConstruct 1–137; UniProt 1–137

V-type proton ATPase subunit S1

OrganismNot specified

UniProt Q15904

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain U; UniProt 1–470 Not recorded V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) Renin receptor × 1 (O75787) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 VAS1_HUMAN
Isoform
PDB entities 13
Chains and sequence ranges Author chain U; PDBConstruct 1–470; UniProt 1–470

Renin receptor

OrganismNot specified

UniProt O75787

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain V; UniProt 1–350 Not recorded V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name RENR_HUMAN
Isoform
PDB entities 14
Chains and sequence ranges Author chain V; PDBConstruct 1–350; UniProt 1–350

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9cf8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9cf8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9cf8
Deposition date deposition_date2024-06-27
Structure title titleCryo-EM structure of human kidney V-ATPase state 1
Keywords keywordshuman, kidney, V-ATPase, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier82.01
Radius of gyration Rg (electron density) rg_electron83.26
Forward intensity I(0) i08254040000.00
Molecular weight molecular_weight800860.0 kDa
Excluded volume excluded_volume1013700 ų
Envelope volume envelope_volume1558100 ų
Hydration-shell volume shell_volume159750 ų
Envelope diameter envelope_diameter280.8
Shell Rg shell_rg77.95
Envelope Rg envelope_rg79.59
Shape Rg shape_rg83.31
Total Rg total_rg83.03
Total atoms total_atoms56307
Residues n_residues7287
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 dmax231.4
Rg (real space) rg_real80.32
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real8.0070e+09
I(0) uncertainty (real space) i0_real_error1.6460e+08
Rg (reciprocal space) rg_reciprocal79.51
I(0) (reciprocal space) i0_reciprocal8196000000.0000
Solution quality estimate total_estimate0.8645
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary60.9
Skewness Skewness skewness0.372
Kurtosis Kurtosis kurtosis-0.824
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha1.4160
Highest regularization parameter α highest_alpha1679000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 0.981; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

8. Citations (1)

9. Files and Curves (10)