6wm2

Human V-ATPase in state 1 with SidK and ADP

Method: ELECTRON MICROSCOPY Dmax: 219.1 Å Quality: EXCELLENT

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

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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) 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 subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) 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 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 1
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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) 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 subunit E 1 × 3 (P36543) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) 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 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 2
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 C 1

OrganismNot specified

UniProt P21283

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain O; UniProt 1–382 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) 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 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATC1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain O; PDBConstruct 1–382; UniProt 1–382

V-type proton ATPase subunit H

OrganismNot specified

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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain P; UniProt 1–483 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) 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 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 4
Chains and sequence ranges Author chain P; PDBConstruct 1–483; UniProt 1–483

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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain R; UniProt 1–837 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) 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 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 5
Chains and sequence ranges Author chain R; PDBConstruct 1–837; UniProt 1–837

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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain A; UniProt 1–617 Chain B; UniProt 1–617 Chain C; UniProt 1–617 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) 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 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 6
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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) 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 subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) 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 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 7
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

SidK

OrganismNot specified

UniProt A0A4T1L9X6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain X; UniProt 1–573 Chain Y; UniProt 1–573 Chain Z; UniProt 1–573 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) 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 F × 1 (Q16864) 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 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name A0A4T1L9X6_LEGPN
Isoform
PDB entities 8
Chains and sequence ranges Author chain X; PDBConstruct 1–573; UniProt 1–573 Author chain Y; PDBConstruct 1–573; UniProt 1–573 Author chain Z; PDBConstruct 1–573; UniProt 1–573

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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain G; UniProt 1–247 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit F × 1 (Q16864) 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 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 9
Chains and sequence ranges Author chain G; PDBConstruct 1–247; UniProt 1–247

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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain N; UniProt 1–119 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) 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 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 10
Chains and sequence ranges Author chain N; PDBConstruct 1–119; UniProt 1–119

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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain 0; UniProt 1–205 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 11
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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) 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 subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 12
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 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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain Q; UniProt 1–351 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) 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 e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 13
Chains and sequence ranges Author chain Q; PDBConstruct 1–351; UniProt 1–351

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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain S; UniProt 1–81 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) 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 d 1 × 1 (P61421) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 14
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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain T; UniProt 1–137 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) 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 d 1 × 1 (P61421) V-type proton ATPase subunit e 1 × 1 (O15342) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 15
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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain U; UniProt 1–470 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) 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 d 1 × 1 (P61421) V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) Renin receptor × 1 (O75787) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 16
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 Other combination Heteromer Protein × 35 其他Polymer 8 PDB declaration: 35-meric(35) Consistent with protein copy count Chain V; UniProt 1–350 Not recorded V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit C 1 × 1 (P21283) V-type proton ATPase subunit H × 1 (Q9UI12) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (Q93050) V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (A0A4T1L9X6) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) 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 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) ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose ; × 1 ;beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 13 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 17
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 6wm2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wm2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wm2
Deposition date deposition_date2020-04-20
Structure title titleHuman V-ATPase in state 1 with SidK and ADP
Keywords keywordsV-ATPase, proton pump, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier83.47
Radius of gyration Rg (electron density) rg_electron84.31
Forward intensity I(0) i013898300000.00
Molecular weight molecular_weight1042600.0 kDa
Excluded volume excluded_volume1320800 ų
Envelope volume envelope_volume2120500 ų
Hydration-shell volume shell_volume210510 ų
Envelope diameter envelope_diameter290.0
Shell Rg shell_rg83.68
Envelope Rg envelope_rg80.14
Shape Rg shape_rg84.32
Total Rg total_rg84.29
Total atoms total_atoms73243
Residues n_residues9171
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 dmax219.1
Rg (real space) rg_real80.43
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real1.3460e+10
I(0) uncertainty (real space) i0_real_error2.4570e+08
Rg (reciprocal space) rg_reciprocal82.45
I(0) (reciprocal space) i0_reciprocal13860000000.0000
Solution quality estimate total_estimate0.9035
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary92.3
Skewness Skewness skewness0.276
Kurtosis Kurtosis kurtosis-0.667
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.1972
Highest regularization parameter α highest_alpha1552000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.980; Stabil: 0.981; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.003

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (29)

7. Fold Classification (SCOP + CATH) 19 domains

SCOP 2.08 (12 domains)

Domain ID domain_idd6wm2d1
Class classb — All beta proteins
Fold Fold foldb.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamilyb.49.1 — N-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family familyb.49.1.0 — automated matches
Domain ID domain_idd6wm2d2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.0 — automated matches
Domain ID domain_idd6wm2d3
Class classa — All alpha proteins
Fold Fold folda.69 — Left-handed superhelix
Superfamily Superfamily superfamilya.69.1 — C-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family familya.69.1.0 — automated matches
Domain ID domain_idd6wm2e1
Class classb — All beta proteins
Fold Fold foldb.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamilyb.49.1 — N-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family familyb.49.1.0 — automated matches
Domain ID domain_idd6wm2e2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.0 — automated matches
Domain ID domain_idd6wm2e3
Class classa — All alpha proteins
Fold Fold folda.69 — Left-handed superhelix
Superfamily Superfamily superfamilya.69.1 — C-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family familya.69.1.0 — automated matches
Domain ID domain_idd6wm2f1
Class classb — All beta proteins
Fold Fold foldb.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamilyb.49.1 — N-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family familyb.49.1.0 — automated matches
Domain ID domain_idd6wm2f2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.0 — automated matches
Domain ID domain_idd6wm2f3
Class classa — All alpha proteins
Fold Fold folda.69 — Left-handed superhelix
Superfamily Superfamily superfamilya.69.1 — C-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family familya.69.1.0 — automated matches
Domain ID domain_idd6wm2g_
Class classh — Coiled coil proteins
Fold Fold foldh.4 — Antiparallel coiled-coil
Superfamily Superfamily superfamilyh.4.20 — V-type ATPase central rotor subunit D
Family Family familyh.4.20.0 — automated matches
Domain ID domain_idd6wm2n_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.149 — AtpF-like
Superfamily Superfamily superfamilyc.149.1 — AtpF-like
Family Family familyc.149.1.0 — automated matches
Domain ID domain_idd6wm2q_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.40 — V-type ATP synthase subunit C
Superfamily Superfamily superfamilyf.40.1 — V-type ATP synthase subunit C
Family Family familyf.40.1.0 — automated matches

CATH v4.4 (7 domains)

Domain ID domain_id6wm2G01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily3240
Domain ID domain_id6wm2H01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily30 — ATP synthase, E subunit, C-terminal
Domain ID domain_id6wm2I01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily30 — ATP synthase, E subunit, C-terminal
Domain ID domain_id6wm2J01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily30 — ATP synthase, E subunit, C-terminal
Domain ID domain_id6wm2K01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily2950
Domain ID domain_id6wm2P01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id6wm2P02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily150 — V-type ATPase, subunit H, C-terminal domain

8. Citations (1)

9. Files and Curves (10)