2xnd

Crystal structure of bovine F1-c8 sub-complex of ATP Synthase

Method: X-RAY DIFFRACTION Dmax: 192.6 Å Quality: GOOD

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

ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL

OrganismNot specified

UniProt P19483

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain A; UniProt 62–553 Chain B; UniProt 62–553 Chain C; UniProt 62–553 Fragment:RESIDUES 62-553 ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL × 8 (P32876) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 GOL GLYCEROL × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;CRYSTALS WERE GROWN UNDER OIL BY MIXING EQUAL VOLUMES OF PROTEIN (10MG/ML IN 20MM TRIS PH 8.0, 10% GLYCEROL, 1MM ADP, 1MM AMP-PNP, 2MM MGSO4, 0.02% NAN3, 5.7MM TDM) AND PRECIPITANT SOLUTION (50MM HEPES PH 7.0, 14% PEG4600, 50MM K2HPO4) Resolution 3.50 Å R-free 0.304

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.

58 other PDB entries and 62 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPA_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–492; UniProt 62–553 Author chain B; PDBConstruct 1–492; UniProt 62–553 Author chain C; PDBConstruct 1–492; UniProt 62–553

ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL

OrganismNot specified

UniProt P00829

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain D; UniProt 59–525 Chain E; UniProt 59–525 Chain F; UniProt 59–525 Fragment:RESIDUES 59-525 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL × 8 (P32876) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 GOL GLYCEROL × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;CRYSTALS WERE GROWN UNDER OIL BY MIXING EQUAL VOLUMES OF PROTEIN (10MG/ML IN 20MM TRIS PH 8.0, 10% GLYCEROL, 1MM ADP, 1MM AMP-PNP, 2MM MGSO4, 0.02% NAN3, 5.7MM TDM) AND PRECIPITANT SOLUTION (50MM HEPES PH 7.0, 14% PEG4600, 50MM K2HPO4) Resolution 3.50 Å R-free 0.304

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.

55 other PDB entries and 59 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPB_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–467; UniProt 59–525 Author chain E; PDBConstruct 1–467; UniProt 59–525 Author chain F; PDBConstruct 1–467; UniProt 59–525

ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL

OrganismNot specified

UniProt P05631

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain G; UniProt 26–297 Fragment:RESIDUES 26-297 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL × 8 (P32876) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 GOL GLYCEROL × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;CRYSTALS WERE GROWN UNDER OIL BY MIXING EQUAL VOLUMES OF PROTEIN (10MG/ML IN 20MM TRIS PH 8.0, 10% GLYCEROL, 1MM ADP, 1MM AMP-PNP, 2MM MGSO4, 0.02% NAN3, 5.7MM TDM) AND PRECIPITANT SOLUTION (50MM HEPES PH 7.0, 14% PEG4600, 50MM K2HPO4) Resolution 3.50 Å R-free 0.304

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.

58 other PDB entries and 62 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPG_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–272; UniProt 26–297

ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL

OrganismNot specified

UniProt P05630

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain H; UniProt 37–167 Fragment:RESIDUES 37-167 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL × 8 (P32876) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 GOL GLYCEROL × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;CRYSTALS WERE GROWN UNDER OIL BY MIXING EQUAL VOLUMES OF PROTEIN (10MG/ML IN 20MM TRIS PH 8.0, 10% GLYCEROL, 1MM ADP, 1MM AMP-PNP, 2MM MGSO4, 0.02% NAN3, 5.7MM TDM) AND PRECIPITANT SOLUTION (50MM HEPES PH 7.0, 14% PEG4600, 50MM K2HPO4) Resolution 3.50 Å R-free 0.304

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.

38 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPD_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–131; UniProt 37–167

ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL

OrganismNot specified

UniProt P05632

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain I; UniProt 2–48 Fragment:RESIDUES 2-48 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL × 8 (P32876) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 GOL GLYCEROL × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;CRYSTALS WERE GROWN UNDER OIL BY MIXING EQUAL VOLUMES OF PROTEIN (10MG/ML IN 20MM TRIS PH 8.0, 10% GLYCEROL, 1MM ADP, 1MM AMP-PNP, 2MM MGSO4, 0.02% NAN3, 5.7MM TDM) AND PRECIPITANT SOLUTION (50MM HEPES PH 7.0, 14% PEG4600, 50MM K2HPO4) Resolution 3.50 Å R-free 0.304

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.

38 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP5E_BOVIN
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–47; UniProt 2–48

ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL

OrganismNot specified

UniProt P32876

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain J; UniProt 63–134 Chain K; UniProt 63–134 Chain L; UniProt 63–134 Chain M; UniProt 63–134 Chain N; UniProt 63–134 Chain O; UniProt 63–134 Chain P; UniProt 63–134 Chain Q; UniProt 63–134 Fragment:RESIDUES 63-134 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 GOL GLYCEROL × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;CRYSTALS WERE GROWN UNDER OIL BY MIXING EQUAL VOLUMES OF PROTEIN (10MG/ML IN 20MM TRIS PH 8.0, 10% GLYCEROL, 1MM ADP, 1MM AMP-PNP, 2MM MGSO4, 0.02% NAN3, 5.7MM TDM) AND PRECIPITANT SOLUTION (50MM HEPES PH 7.0, 14% PEG4600, 50MM K2HPO4) Resolution 3.50 Å R-free 0.304

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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AT5G1_BOVIN
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–72; UniProt 63–134 Author chain K; PDBConstruct 1–72; UniProt 63–134 Author chain L; PDBConstruct 1–72; UniProt 63–134 Author chain M; PDBConstruct 1–72; UniProt 63–134 Author chain N; PDBConstruct 1–72; UniProt 63–134 Author chain O; PDBConstruct 1–72; UniProt 63–134 Author chain P; PDBConstruct 1–72; UniProt 63–134 Author chain Q; PDBConstruct 1–72; UniProt 63–134

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 2xnd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2xnd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2xnd
Deposition date deposition_date2010-08-02
Structure title titleCrystal structure of bovine F1-c8 sub-complex of ATP Synthase
Keywords keywordsATP PHOSPHORYLASE (H+ TRANSPORTING), ATP SYNTHESIS, F1FO ATP SYNTHASE, HYDROLASE, ION TRANSPORT, P-LOOP; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier54.65
Radius of gyration Rg (electron density) rg_electron53.49
Forward intensity I(0) i02381370000.00
Molecular weight molecular_weight400790.0 kDa
Excluded volume excluded_volume499260 ų
Envelope volume envelope_volume680670 ų
Hydration-shell volume shell_volume108510 ų
Envelope diameter envelope_diameter213.3
Shell Rg shell_rg55.89
Envelope Rg envelope_rg54.36
Shape Rg shape_rg53.68
Total Rg total_rg52.90
Total atoms total_atoms28196
Residues n_residues3892
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 dmax192.6
Rg (real space) rg_real55.19
Rg uncertainty (real space) rg_real_error1.91
I(0) (real space) i0_real2.3810e+09
I(0) uncertainty (real space) i0_real_error4.7880e+07
Rg (reciprocal space) rg_reciprocal54.20
I(0) (reciprocal space) i0_reciprocal2378000000.0000
Solution quality estimate total_estimate0.7721
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.8
Skewness Skewness skewness0.758
Kurtosis Kurtosis kurtosis0.238
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha381700000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.548; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.402

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 31 domains

CATH v4.4 (31 domains)

Domain ID domain_id2xndA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id2xndA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2xndA03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology150 — Lysin
Homologous superfamily homologous superfamily20 — ATP synthase alpha/beta chain, C-terminal domain
Domain ID domain_id2xndB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id2xndB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2xndB03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology150 — Lysin
Homologous superfamily homologous superfamily20 — ATP synthase alpha/beta chain, C-terminal domain
Domain ID domain_id2xndC01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id2xndC02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2xndC03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology150 — Lysin
Homologous superfamily homologous superfamily20 — ATP synthase alpha/beta chain, C-terminal domain
Domain ID domain_id2xndD01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id2xndD02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2xndD03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1140 — Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3
Homologous superfamily homologous superfamily10 — Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3
Domain ID domain_id2xndE01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id2xndE02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2xndE03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1140 — Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3
Homologous superfamily homologous superfamily10 — Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3
Domain ID domain_id2xndF01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id2xndF02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2xndF03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1140 — Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3
Homologous superfamily homologous superfamily10 — Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3
Domain ID domain_id2xndG01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily80 — ATP synthase, gamma subunit, helix hairpin domain
Domain ID domain_id2xndG02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily10 — ATP synthase, F1 complex, gamma subunit
Domain ID domain_id2xndH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology15 — ATP Synthase; domain 1
Homologous superfamily homologous superfamily10 — F0F1 ATP synthase delta/epsilon subunit, N-terminal
Domain ID domain_id2xndH02
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 superfamily440 — ATP synthase delta/epsilon subunit, C-terminal domain
Domain ID domain_id2xndI00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1620 — Atp Synthase Epsilon Chain; Chain: I;
Homologous superfamily homologous superfamily20 — ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial
Domain ID domain_id2xndJ00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id2xndK00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id2xndL00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id2xndM00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id2xndN00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id2xndO00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id2xndP00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id2xndQ00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C

8. Citations (1)

9. Files and Curves (10)