6m0r

2.7A Yeast Vo state3

Method: ELECTRON MICROSCOPY Dmax: 139.5 Å Quality: GOOD

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

;V-type proton ATPase subunit c' ;

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P32842

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 15 其他Polymer 1 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain D; UniProt 7–164 Not recorded ;V-type proton ATPase subunit c'' ; × 1 (P23968) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ;alpha-D-mannopyranose-(1-3)-[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 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 30 PPV PYROPHOSPHATE × 1 EYR (6~{E},10~{E},14~{E},18~{E},22~{E},26~{E},30~{R})-2,6,10,14,18,22,26,30-octamethyldotriaconta-2,6,10,14,18,22,26-heptaene × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 Å

Other States of the Same Protein in the Database

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

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–158; UniProt 7–164

;V-type proton ATPase subunit c'' ;

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P23968

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 15 其他Polymer 1 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain C; UniProt 16–213 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ;alpha-D-mannopyranose-(1-3)-[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 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 30 PPV PYROPHOSPHATE × 1 EYR (6~{E},10~{E},14~{E},18~{E},22~{E},26~{E},30~{R})-2,6,10,14,18,22,26,30-octamethyldotriaconta-2,6,10,14,18,22,26-heptaene × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 Å

Other States of the Same Protein in the Database

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

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATO_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–198; UniProt 16–213

V0 assembly protein 1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P53262

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 15 其他Polymer 1 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain N; UniProt 212–263 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ;alpha-D-mannopyranose-(1-3)-[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 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 30 PPV PYROPHOSPHATE × 1 EYR (6~{E},10~{E},14~{E},18~{E},22~{E},26~{E},30~{R})-2,6,10,14,18,22,26,30-octamethyldotriaconta-2,6,10,14,18,22,26-heptaene × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 Å

Other States of the Same Protein in the Database

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

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VOA1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain N; PDBConstruct 1–52; UniProt 212–263

V-type proton ATPase subunit e

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt Q3E7B6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 15 其他Polymer 1 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain M; UniProt 1–71 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit c × 8 (P25515) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ;alpha-D-mannopyranose-(1-3)-[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 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 30 PPV PYROPHOSPHATE × 1 EYR (6~{E},10~{E},14~{E},18~{E},22~{E},26~{E},30~{R})-2,6,10,14,18,22,26,30-octamethyldotriaconta-2,6,10,14,18,22,26-heptaene × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 Å

Other States of the Same Protein in the Database

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

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0E_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain M; PDBConstruct 1–71; UniProt 1–71

V-type proton ATPase subunit c

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 Other combination Heteromer Protein × 15 其他Polymer 1 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain E; UniProt 1–159 Chain F; UniProt 1–159 Chain G; UniProt 1–159 Chain H; UniProt 1–159 Chain I; UniProt 1–159 Chain J; UniProt 1–159 Chain K; UniProt 1–159 Chain L; UniProt 1–159 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit e × 1 (Q3E7B6) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ;alpha-D-mannopyranose-(1-3)-[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 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 30 PPV PYROPHOSPHATE × 1 EYR (6~{E},10~{E},14~{E},18~{E},22~{E},26~{E},30~{R})-2,6,10,14,18,22,26,30-octamethyldotriaconta-2,6,10,14,18,22,26-heptaene × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 5
Chains and sequence ranges Author chain E; PDBConstruct 1–159; UniProt 1–159 Author chain F; PDBConstruct 1–159; UniProt 1–159 Author chain G; PDBConstruct 1–159; UniProt 1–159 Author chain H; PDBConstruct 1–159; UniProt 1–159 Author chain I; PDBConstruct 1–159; UniProt 1–159 Author chain J; PDBConstruct 1–159; UniProt 1–159 Author chain K; PDBConstruct 1–159; UniProt 1–159 Author chain L; PDBConstruct 1–159; UniProt 1–159

Uncharacterized protein YPR170W-B

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P0C5R9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 15 其他Polymer 1 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain O; UniProt 7–75 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ;alpha-D-mannopyranose-(1-3)-[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 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 30 PPV PYROPHOSPHATE × 1 EYR (6~{E},10~{E},14~{E},18~{E},22~{E},26~{E},30~{R})-2,6,10,14,18,22,26,30-octamethyldotriaconta-2,6,10,14,18,22,26-heptaene × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name YP17B_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain O; PDBConstruct 1–69; UniProt 7–75

V-type proton ATPase subunit d

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 Other combination Heteromer Protein × 15 其他Polymer 1 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain B; UniProt 1–345 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ;alpha-D-mannopyranose-(1-3)-[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 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 30 PPV PYROPHOSPHATE × 1 EYR (6~{E},10~{E},14~{E},18~{E},22~{E},26~{E},30~{R})-2,6,10,14,18,22,26,30-octamethyldotriaconta-2,6,10,14,18,22,26-heptaene × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 7
Chains and sequence ranges Author chain B; PDBConstruct 1–345; UniProt 1–345

V-type proton ATPase subunit a, vacuolar isoform

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 Other combination Heteromer Protein × 15 其他Polymer 1 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 3–827 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) ;alpha-D-mannopyranose-(1-3)-[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 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 30 PPV PYROPHOSPHATE × 1 EYR (6~{E},10~{E},14~{E},18~{E},22~{E},26~{E},30~{R})-2,6,10,14,18,22,26,30-octamethyldotriaconta-2,6,10,14,18,22,26-heptaene × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 8
Chains and sequence ranges Author chain A; PDBConstruct 1–825; UniProt 3–827

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 6m0r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6m0r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6m0r
Deposition date deposition_date2020-02-22
Structure title title2.7A Yeast Vo state3
Keywords keywordsV-ATPase, Vo sub-complex, CryoEM, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.08
Radius of gyration Rg (electron density) rg_electron43.91
Forward intensity I(0) i01296960000.00
Molecular weight molecular_weight334120.0 kDa
Excluded volume excluded_volume432760 ų
Envelope volume envelope_volume585480 ų
Hydration-shell volume shell_volume103910 ų
Envelope diameter envelope_diameter147.2
Shell Rg shell_rg54.07
Envelope Rg envelope_rg43.23
Shape Rg shape_rg43.93
Total Rg total_rg44.26
Total atoms total_atoms47976
Residues n_residues2915
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 dmax139.5
Rg (real space) rg_real44.75
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real1.2970e+09
I(0) uncertainty (real space) i0_real_error2.1380e+07
Rg (reciprocal space) rg_reciprocal45.08
I(0) (reciprocal space) i0_reciprocal1297000000.0000
Solution quality estimate total_estimate0.8911
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.8
Skewness Skewness skewness0.081
Kurtosis Kurtosis kurtosis-0.500
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha136700000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

7. Fold Classification (SCOP + CATH) 19 domains

SCOP 2.08 (19 domains)

Domain ID domain_idd6m0rb_
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_idd6m0rd1
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_idd6m0rd2
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.17.1.0 — automated matches
Domain ID domain_idd6m0re1
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_idd6m0re2
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_idd6m0rf1
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_idd6m0rf2
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_idd6m0rg1
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_idd6m0rg2
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_idd6m0rh1
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_idd6m0rh2
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_idd6m0ri1
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_idd6m0ri2
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_idd6m0rj1
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_idd6m0rj2
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_idd6m0rk1
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_idd6m0rk2
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_idd6m0rl1
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_idd6m0rl2
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

8. Citations (1)

9. Files and Curves (10)