1h8e

(ADP.AlF4)2(ADP.SO4) bovine F1-ATPase (all three catalytic sites occupied)

Method: X-RAY DIFFRACTION Dmax: 143.5 Å Quality: GOOD

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

BOVINE MITOCHONDRIAL F1-ATPASE

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 44–553 Chain B; UniProt 44–553 Chain C; UniProt 44–553 Not recorded BOVINE MITOCHONDRIAL F1-ATPASE × 3 (P00829) BOVINE MITOCHONDRIAL F1-ATPASE × 1 (P05631) BOVINE MITOCHONDRIAL F1-ATPASE × 1 (P05630) BOVINE MITOCHONDRIAL F1-ATPASE × 1 (P05632) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 GOL GLYCEROL × 4 ALF TETRAFLUOROALUMINATE ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;CRYSTALS WERE GROWN IN THE PRESENCE OF AZIDE, A KNOWN INHIBITOR, BUT THIS HAS NOT BEEN LOCATED IN THE STRUCTURE., pH 8.00 Resolution 2.00 Å R-free 0.264

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 ATP0_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–510; UniProt 44–553 Author chain B; PDBConstruct 1–510; UniProt 44–553 Author chain C; PDBConstruct 1–510; UniProt 44–553

BOVINE MITOCHONDRIAL F1-ATPASE

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain D; UniProt 47–528 Chain E; UniProt 47–528 Chain F; UniProt 47–528 Not recorded BOVINE MITOCHONDRIAL F1-ATPASE × 3 (P19483) BOVINE MITOCHONDRIAL F1-ATPASE × 1 (P05631) BOVINE MITOCHONDRIAL F1-ATPASE × 1 (P05630) BOVINE MITOCHONDRIAL F1-ATPASE × 1 (P05632) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 GOL GLYCEROL × 4 ALF TETRAFLUOROALUMINATE ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;CRYSTALS WERE GROWN IN THE PRESENCE OF AZIDE, A KNOWN INHIBITOR, BUT THIS HAS NOT BEEN LOCATED IN THE STRUCTURE., pH 8.00 Resolution 2.00 Å R-free 0.264

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 1–482; UniProt 47–528 Author chain E; PDBConstruct 1–482; UniProt 47–528 Author chain F; PDBConstruct 1–482; UniProt 47–528

BOVINE MITOCHONDRIAL F1-ATPASE

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain G; UniProt 26–297 Not recorded BOVINE MITOCHONDRIAL F1-ATPASE × 3 (P19483) BOVINE MITOCHONDRIAL F1-ATPASE × 3 (P00829) BOVINE MITOCHONDRIAL F1-ATPASE × 1 (P05630) BOVINE MITOCHONDRIAL F1-ATPASE × 1 (P05632) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 GOL GLYCEROL × 4 ALF TETRAFLUOROALUMINATE ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;CRYSTALS WERE GROWN IN THE PRESENCE OF AZIDE, A KNOWN INHIBITOR, BUT THIS HAS NOT BEEN LOCATED IN THE STRUCTURE., pH 8.00 Resolution 2.00 Å R-free 0.264

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

BOVINE MITOCHONDRIAL F1-ATPASE

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain H; UniProt 23–168 Not recorded BOVINE MITOCHONDRIAL F1-ATPASE × 3 (P19483) BOVINE MITOCHONDRIAL F1-ATPASE × 3 (P00829) BOVINE MITOCHONDRIAL F1-ATPASE × 1 (P05631) BOVINE MITOCHONDRIAL F1-ATPASE × 1 (P05632) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 GOL GLYCEROL × 4 ALF TETRAFLUOROALUMINATE ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;CRYSTALS WERE GROWN IN THE PRESENCE OF AZIDE, A KNOWN INHIBITOR, BUT THIS HAS NOT BEEN LOCATED IN THE STRUCTURE., pH 8.00 Resolution 2.00 Å R-free 0.264

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 1–146; UniProt 23–168

BOVINE MITOCHONDRIAL F1-ATPASE

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain I; UniProt 1–50 Not recorded BOVINE MITOCHONDRIAL F1-ATPASE × 3 (P19483) BOVINE MITOCHONDRIAL F1-ATPASE × 3 (P00829) BOVINE MITOCHONDRIAL F1-ATPASE × 1 (P05631) BOVINE MITOCHONDRIAL F1-ATPASE × 1 (P05630) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 GOL GLYCEROL × 4 ALF TETRAFLUOROALUMINATE ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;CRYSTALS WERE GROWN IN THE PRESENCE OF AZIDE, A KNOWN INHIBITOR, BUT THIS HAS NOT BEEN LOCATED IN THE STRUCTURE., pH 8.00 Resolution 2.00 Å R-free 0.264

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 ATPE_BOVIN
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–50; UniProt 1–50

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 1h8e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1h8e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1h8e
Deposition date deposition_date2001-02-02
Structure title title(ADP.AlF4)2(ADP.SO4) bovine F1-ATPase (all three catalytic sites occupied)
Keywords keywordsHYDROLASE, ATP PHOSPHORYLASE, ATP PHOSPHORYLASE (H+ TRANSPORTING), ATP SYNTHASE, F1FO ATP SYNTHASE, F1-ATPASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.31
Radius of gyration Rg (electron density) rg_electron43.62
Forward intensity I(0) i01756500000.00
Molecular weight molecular_weight350730.0 kDa
Excluded volume excluded_volume440760 ų
Envelope volume envelope_volume568640 ų
Hydration-shell volume shell_volume101920 ų
Envelope diameter envelope_diameter155.0
Shell Rg shell_rg53.41
Envelope Rg envelope_rg43.34
Shape Rg shape_rg43.64
Total Rg total_rg43.90
Total atoms total_atoms24636
Residues n_residues3209
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 dmax143.5
Rg (real space) rg_real44.06
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real1.7560e+09
I(0) uncertainty (real space) i0_real_error2.9930e+07
Rg (reciprocal space) rg_reciprocal44.31
I(0) (reciprocal space) i0_reciprocal1757000000.0000
Solution quality estimate total_estimate0.8728
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.174
Kurtosis Kurtosis kurtosis-0.314
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha437800000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.898

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 42 domains

SCOP 2.08 (21 domains)

Domain ID domain_idd1h8ea1
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.69.1.1 — C-terminal domain of alpha and beta subunits of F1 ATP synthase
Domain ID domain_idd1h8ea2
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.49.1.1 — N-terminal domain of alpha and beta subunits of F1 ATP synthase
Domain ID domain_idd1h8ea3
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_idd1h8eb1
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.69.1.1 — C-terminal domain of alpha and beta subunits of F1 ATP synthase
Domain ID domain_idd1h8eb2
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.49.1.1 — N-terminal domain of alpha and beta subunits of F1 ATP synthase
Domain ID domain_idd1h8eb3
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_idd1h8ec1
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.69.1.1 — C-terminal domain of alpha and beta subunits of F1 ATP synthase
Domain ID domain_idd1h8ec2
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.49.1.1 — N-terminal domain of alpha and beta subunits of F1 ATP synthase
Domain ID domain_idd1h8ec3
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_idd1h8ed1
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.69.1.1 — C-terminal domain of alpha and beta subunits of F1 ATP synthase
Domain ID domain_idd1h8ed2
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.49.1.1 — N-terminal domain of alpha and beta subunits of F1 ATP synthase
Domain ID domain_idd1h8ed3
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_idd1h8ee1
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.69.1.1 — C-terminal domain of alpha and beta subunits of F1 ATP synthase
Domain ID domain_idd1h8ee2
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.49.1.1 — N-terminal domain of alpha and beta subunits of F1 ATP synthase
Domain ID domain_idd1h8ee3
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_idd1h8ef1
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.69.1.1 — C-terminal domain of alpha and beta subunits of F1 ATP synthase
Domain ID domain_idd1h8ef2
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.49.1.1 — N-terminal domain of alpha and beta subunits of F1 ATP synthase
Domain ID domain_idd1h8ef3
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_idd1h8eg_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.49 — Pyruvate kinase C-terminal domain-like
Superfamily Superfamily superfamilyc.49.2 — ATP synthase (F1-ATPase), gamma subunit
Family Family familyc.49.2.1 — ATP synthase (F1-ATPase), gamma subunit
Domain ID domain_idd1h8eh_
Class classb — All beta proteins
Fold Fold foldb.93 — Epsilon subunit of F1F0-ATP synthase N-terminal domain
Superfamily Superfamily superfamilyb.93.1 — Epsilon subunit of F1F0-ATP synthase N-terminal domain
Family Family familyb.93.1.1 — Epsilon subunit of F1F0-ATP synthase N-terminal domain
Domain ID domain_idd1h8ei_
Class classa — All alpha proteins
Fold Fold folda.137 — Non-globular all-alpha subunits of globular proteins
Superfamily Superfamily superfamilya.137.8 — Epsilon subunit of mitochondrial F1F0-ATP synthase
Family Family familya.137.8.1 — Epsilon subunit of mitochondrial F1F0-ATP synthase

CATH v4.4 (21 domains)

Domain ID domain_id1h8eA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id1h8eA02
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_id1h8eA03
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_id1h8eB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id1h8eB02
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_id1h8eB03
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_id1h8eC01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id1h8eC02
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_id1h8eC03
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_id1h8eD01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id1h8eD02
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_id1h8eD03
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_id1h8eE01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id1h8eE02
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_id1h8eE03
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_id1h8eF01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id1h8eF02
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_id1h8eF03
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_id1h8eG01
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_id1h8eG02
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_id1h8eH00
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

8. Citations (6)

9. Files and Curves (10)