6wlw

The Vo region of human V-ATPase in state 1 (focused refinement)

Method: ELECTRON MICROSCOPY Dmax: 137.0 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 Other combination Heteromer Protein × 16 其他Polymer 8 PDB declaration: hexadecameric(16) 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 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) ;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 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 PTY PHOSPHATIDYLETHANOLAMINE × 13 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 Other combination Heteromer Protein × 16 其他Polymer 8 PDB declaration: hexadecameric(16) 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 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) ;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 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 PTY PHOSPHATIDYLETHANOLAMINE × 13 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 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 × 16 其他Polymer 8 PDB declaration: hexadecameric(16) 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 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) ;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 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 PTY PHOSPHATIDYLETHANOLAMINE × 13 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 3
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 Other combination Heteromer Protein × 16 其他Polymer 8 PDB declaration: hexadecameric(16) 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 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 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 PTY PHOSPHATIDYLETHANOLAMINE × 13 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 4
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 Other combination Heteromer Protein × 16 其他Polymer 8 PDB declaration: hexadecameric(16) 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 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) ;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 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 PTY PHOSPHATIDYLETHANOLAMINE × 13 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 5
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 × 16 其他Polymer 8 PDB declaration: hexadecameric(16) 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 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) ;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 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 PTY PHOSPHATIDYLETHANOLAMINE × 13 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 6
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 × 16 其他Polymer 8 PDB declaration: hexadecameric(16) 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 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) ;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 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 PTY PHOSPHATIDYLETHANOLAMINE × 13 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 7
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 × 16 其他Polymer 8 PDB declaration: hexadecameric(16) 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 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) ;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 WSS tri(methyl)-[2-[[(2~{R})-2-[(~{Z})-octadec-9-enoyl]oxy-3-[(~{E})-1-oxidanylideneoctadec-9-enoxy]propoxy]-oxidanyl-phosphoryl]oxyethyl]azanium × 10 PTY PHOSPHATIDYLETHANOLAMINE × 13 WJS (2~{S})-2-$l^{4}-azanyl-3-[[(2~{R})-3-octadecanoyloxy-2-oxidanyl-propoxy]-oxidanyl-oxidanylidene-$l^{6}-phosphanyl]oxy-propanoic acid × 1 CLR CHOLESTEROL × 4 PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE × 1 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 8
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 6wlw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6wlw
Deposition date deposition_date2020-04-20
Structure title titleThe Vo region of human V-ATPase in state 1 (focused refinement)
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_guinier43.96
Radius of gyration Rg (electron density) rg_electron42.76
Forward intensity I(0) i01161390000.00
Molecular weight molecular_weight315040.0 kDa
Excluded volume excluded_volume407760 ų
Envelope volume envelope_volume527310 ų
Hydration-shell volume shell_volume96742 ų
Envelope diameter envelope_diameter145.6
Shell Rg shell_rg51.98
Envelope Rg envelope_rg42.35
Shape Rg shape_rg42.79
Total Rg total_rg43.04
Total atoms total_atoms22145
Residues n_residues2749
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 dmax137.0
Rg (real space) rg_real43.69
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real1.1610e+09
I(0) uncertainty (real space) i0_real_error2.0640e+07
Rg (reciprocal space) rg_reciprocal43.95
I(0) (reciprocal space) i0_reciprocal1162000000.0000
Solution quality estimate total_estimate0.8872
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.1
Skewness Skewness skewness0.124
Kurtosis Kurtosis kurtosis-0.457
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha138500000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.876

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (19)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6wlwq_
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

8. Citations (1)

9. Files and Curves (10)