3j9t

Yeast V-ATPase state 1

Method: ELECTRON MICROSCOPY Dmax: 258.7 Å Quality: GOOD

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

V-type proton ATPase subunit D

OrganismNot specified

UniProt P32610

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain M; UniProt 1–256 Not recorded V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 6.90 Å

Other States of the Same Protein in the Database

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

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

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

V-type proton ATPase subunit F

OrganismNot specified

UniProt P39111

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain N; UniProt 1–118 Not recorded V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 6.90 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name VATF_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain N; PDBConstruct 1–118; UniProt 1–118

V-type proton ATPase catalytic subunit A

OrganismNot specified

UniProt P17255

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain A; UniProt 2–283 Chain A; UniProt 738–1071 Chain C; UniProt 2–283 Chain C; UniProt 738–1071 Chain E; UniProt 2–283 Chain E; UniProt 738–1071 Fragment:SEE REMARK 999 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 6.90 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.

15 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATA_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–282; UniProt 2–283 Author chain A; PDBConstruct 283–616; UniProt 738–1071 Author chain C; PDBConstruct 1–282; UniProt 2–283 Author chain C; PDBConstruct 283–616; UniProt 738–1071 Author chain E; PDBConstruct 1–282; UniProt 2–283 Author chain E; PDBConstruct 283–616; UniProt 738–1071

V-type proton ATPase subunit B

OrganismNot specified

UniProt P16140

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain B; UniProt 1–517 Chain D; UniProt 1–517 Chain F; UniProt 1–517 Not recorded V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 6.90 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name VATB_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–517; UniProt 1–517 Author chain D; PDBConstruct 1–517; UniProt 1–517 Author chain F; PDBConstruct 1–517; UniProt 1–517

V-type proton ATPase subunit d

OrganismNot specified

UniProt P32366

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain Q; UniProt 1–345 Not recorded V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 6.90 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name VA0D_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain Q; PDBConstruct 1–345; UniProt 1–345

V-type proton ATPase subunit G

OrganismNot specified

UniProt P48836

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain H; UniProt 1–114 Chain J; UniProt 1–114 Chain L; UniProt 1–114 Not recorded V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 6.90 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name VATG_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain H; PDBConstruct 1–114; UniProt 1–114 Author chain J; PDBConstruct 1–114; UniProt 1–114 Author chain L; PDBConstruct 1–114; UniProt 1–114

V-type proton ATPase subunit E

OrganismNot specified

UniProt P22203

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain G; UniProt 1–233 Chain I; UniProt 1–233 Chain K; UniProt 1–233 Not recorded V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 6.90 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name VATE_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–233; UniProt 1–233 Author chain I; PDBConstruct 1–233; UniProt 1–233 Author chain K; PDBConstruct 1–233; UniProt 1–233

V-type proton ATPase subunit H

OrganismNot specified

UniProt P41807

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain P; UniProt 1–478 Not recorded V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 6.90 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name VATH_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain P; PDBConstruct 1–478; UniProt 1–478

V-type proton ATPase subunit a, vacuolar isoform

OrganismNot specified

UniProt P32563

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain b; UniProt 1–840 Not recorded V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 6.90 Å

Other States of the Same Protein in the Database

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

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

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

V-type proton ATPase subunit C

OrganismNot specified

UniProt P31412

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain O; UniProt 1–392 Not recorded V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit c × 10 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 6.90 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name VATC_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain O; PDBConstruct 1–392; UniProt 1–392

V-type proton ATPase subunit c

OrganismNot specified

UniProt P25515

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain R; UniProt 1–160 Chain S; UniProt 1–160 Chain T; UniProt 1–160 Chain U; UniProt 1–160 Chain V; UniProt 1–160 Chain W; UniProt 1–160 Chain X; UniProt 1–160 Chain Y; UniProt 1–160 Chain Z; UniProt 1–160 Chain a; UniProt 1–160 Not recorded V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit C × 1 (P31412) ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside;pH 7.4;50 mM Tris-HCl, 150 mM NaCl, 0.02% w/v dodecylmaltoside cryo-EM vitrification conditions:Blot for 23 seconds before freezing;77 K;Cryogen OTHER;Blot for 23 seconds before freezing in ethane/propane mixture (FEI VITROBOT MARK III). Resolution 6.90 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name VATL1_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain R; PDBConstruct 1–160; UniProt 1–160 Author chain S; PDBConstruct 1–160; UniProt 1–160 Author chain T; PDBConstruct 1–160; UniProt 1–160 Author chain U; PDBConstruct 1–160; UniProt 1–160 Author chain V; PDBConstruct 1–160; UniProt 1–160 Author chain W; PDBConstruct 1–160; UniProt 1–160 Author chain X; PDBConstruct 1–160; UniProt 1–160 Author chain Y; PDBConstruct 1–160; UniProt 1–160 Author chain Z; PDBConstruct 1–160; UniProt 1–160 Author chain a; PDBConstruct 1–160; UniProt 1–160

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 3j9t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j9t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j9t
Deposition date deposition_date2015-02-23
Structure title titleYeast V-ATPase state 1
Keywords keywordsV-ATPase, V-type ATPase, vacuolar-type ATPase, proton pump, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier74.39
Radius of gyration Rg (electron density) rg_electron75.24
Forward intensity I(0) i08741930000.00
Molecular weight molecular_weight819230.0 kDa
Excluded volume excluded_volume1036300 ų
Envelope volume envelope_volume1591500 ų
Hydration-shell volume shell_volume177130 ų
Envelope diameter envelope_diameter251.9
Shell Rg shell_rg75.33
Envelope Rg envelope_rg72.41
Shape Rg shape_rg75.20
Total Rg total_rg75.39
Total atoms total_atoms57659
Residues n_residues7451
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 dmax258.7
Rg (real space) rg_real77.93
Rg uncertainty (real space) rg_real_error1.35
I(0) (real space) i0_real8.7590e+09
I(0) uncertainty (real space) i0_real_error1.6850e+08
Rg (reciprocal space) rg_reciprocal73.78
I(0) (reciprocal space) i0_reciprocal8728000000.0000
Solution quality estimate total_estimate0.8756
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary73.9
Skewness Skewness skewness0.504
Kurtosis Kurtosis kurtosis-0.248
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha1.3100
Highest regularization parameter α highest_alpha1398000000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 0.873; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.231

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 53 domains

SCOP 2.08 (53 domains)

Domain ID domain_idd3j9ta1
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.49.1.2 — N-terminal domain of A and B subunits of V1 ATP synthase
Domain ID domain_idd3j9ta2
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.37.1.11 — RecA protein-like (ATPase-domain)
Domain ID domain_idd3j9ta3
Class classb — All beta proteins
Fold Fold foldb.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamilyb.84.5 — V1 ATP synthase A subunit, bulge domain-like
Family Family familyb.84.5.1 — V1 ATP synthase A subunit, bulge domain-like
Domain ID domain_idd3j9ta4
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.69.1.2 — C-terminal domain of A and B subunits of V1 ATP synthase and A1 ATP sythase
Domain ID domain_idd3j9tb1
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.49.1.2 — N-terminal domain of A and B subunits of V1 ATP synthase
Domain ID domain_idd3j9tb2
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.37.1.11 — RecA protein-like (ATPase-domain)
Domain ID domain_idd3j9tb3
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.69.1.2 — C-terminal domain of A and B subunits of V1 ATP synthase and A1 ATP sythase
Domain ID domain_idd3j9tc1
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.49.1.2 — N-terminal domain of A and B subunits of V1 ATP synthase
Domain ID domain_idd3j9tc2
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.37.1.11 — RecA protein-like (ATPase-domain)
Domain ID domain_idd3j9tc3
Class classb — All beta proteins
Fold Fold foldb.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamilyb.84.5 — V1 ATP synthase A subunit, bulge domain-like
Family Family familyb.84.5.1 — V1 ATP synthase A subunit, bulge domain-like
Domain ID domain_idd3j9tc4
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.69.1.2 — C-terminal domain of A and B subunits of V1 ATP synthase and A1 ATP sythase
Domain ID domain_idd3j9td1
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.49.1.2 — N-terminal domain of A and B subunits of V1 ATP synthase
Domain ID domain_idd3j9td2
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.37.1.11 — RecA protein-like (ATPase-domain)
Domain ID domain_idd3j9td3
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.69.1.2 — C-terminal domain of A and B subunits of V1 ATP synthase and A1 ATP sythase
Domain ID domain_idd3j9te1
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.49.1.2 — N-terminal domain of A and B subunits of V1 ATP synthase
Domain ID domain_idd3j9te2
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.37.1.11 — RecA protein-like (ATPase-domain)
Domain ID domain_idd3j9te3
Class classb — All beta proteins
Fold Fold foldb.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamilyb.84.5 — V1 ATP synthase A subunit, bulge domain-like
Family Family familyb.84.5.1 — V1 ATP synthase A subunit, bulge domain-like
Domain ID domain_idd3j9te4
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.69.1.2 — C-terminal domain of A and B subunits of V1 ATP synthase and A1 ATP sythase
Domain ID domain_idd3j9tf1
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.49.1.2 — N-terminal domain of A and B subunits of V1 ATP synthase
Domain ID domain_idd3j9tf2
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.37.1.11 — RecA protein-like (ATPase-domain)
Domain ID domain_idd3j9tf3
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.69.1.2 — C-terminal domain of A and B subunits of V1 ATP synthase and A1 ATP sythase
Domain ID domain_idd3j9tg1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.81 — FwdE/GAPDH domain-like
Superfamily Superfamily superfamilyd.81.4 — V-type ATPase subunit E-like
Family Family familyd.81.4.1 — V-type ATPase subunit E C-terminal domain
Domain ID domain_idd3j9tg2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.36 — V-type ATPase peripheral stalk subunit E coiled coil
Family Family familyh.1.36.1 — V-type ATPase peripheral stalk subunit E coiled coil
Domain ID domain_idd3j9th_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.37 — V-type ATPase peripheral stalk subunit G coiled coil
Family Family familyh.1.37.1 — V-type ATPase peripheral stalk subunit G coiled coil
Domain ID domain_idd3j9ti1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.81 — FwdE/GAPDH domain-like
Superfamily Superfamily superfamilyd.81.4 — V-type ATPase subunit E-like
Family Family familyd.81.4.1 — V-type ATPase subunit E C-terminal domain
Domain ID domain_idd3j9ti2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.36 — V-type ATPase peripheral stalk subunit E coiled coil
Family Family familyh.1.36.1 — V-type ATPase peripheral stalk subunit E coiled coil
Domain ID domain_idd3j9tj_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.37 — V-type ATPase peripheral stalk subunit G coiled coil
Family Family familyh.1.37.1 — V-type ATPase peripheral stalk subunit G coiled coil
Domain ID domain_idd3j9tk1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.81 — FwdE/GAPDH domain-like
Superfamily Superfamily superfamilyd.81.4 — V-type ATPase subunit E-like
Family Family familyd.81.4.1 — V-type ATPase subunit E C-terminal domain
Domain ID domain_idd3j9tk2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.36 — V-type ATPase peripheral stalk subunit E coiled coil
Family Family familyh.1.36.1 — V-type ATPase peripheral stalk subunit E coiled coil
Domain ID domain_idd3j9tl_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.37 — V-type ATPase peripheral stalk subunit G coiled coil
Family Family familyh.1.37.1 — V-type ATPase peripheral stalk subunit G coiled coil
Domain ID domain_idd3j9tm_
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.4.20.1 — V1 ATP synthase D subunit
Domain ID domain_idd3j9tn_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.149 — AtpF-like
Superfamily Superfamily superfamilyc.149.1 — AtpF-like
Family Family familyc.149.1.1 — AtpF-like
Domain ID domain_idd3j9to_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.57 — Vacuolar ATP synthase subunit C
Superfamily Superfamily superfamilye.57.1 — Vacuolar ATP synthase subunit C
Family Family familye.57.1.1 — Vacuolar ATP synthase subunit C
Domain ID domain_idd3j9tp_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.9 — Regulatory subunit H of the V-type ATPase
Domain ID domain_idd3j9tq_
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.40.1.1 — V-type ATP synthase subunit C
Domain ID domain_idd3j9tr1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tr2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9ts1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9ts2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tt1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tt2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tu1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tu2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tv1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tv2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tw1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tw2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tx1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tx2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9ty1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9ty2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tz1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd3j9tz2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

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