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8f2k

Structure of yeast F1-ATPase determined with 100 micromolar cruentaren A

Method: ELECTRON MICROSCOPY Dmax: 127.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ATP synthase subunit alpha

OrganismNot specified

UniProt A0A6A5Q4L9

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 × 7 PDB declaration: heptameric（7） Consistent with protein copy count Chain A； UniProt 61–545 Chain B； UniProt 61–545 Chain C； UniProt 61–545 Not recorded ATP synthase subunit beta × 3 （A0A6A5PX46） ATP synthase subunit gamma × 1 （A0A6A5Q493） ATP ADENOSINE-5'-TRIPHOSPHATE × 5 MG MAGNESIUM ION × 5 XBC Cruentaren A × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE Resolution 2.90 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.

Other PDB Difference from Current Entry 8F2K Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7MD2 The F1 region of ammocidin-bound Saccharomyces cerevisiae ATP synthase Deposited 2021-04-03 Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 36–545（510 aa）
Chain B 36–545（510 aa）
Chain C 36–545（510 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 PO4 PHOSPHATE ION × 1 ZHD (3~{E},5~{Z},7~{E},9~{R},10~{S},11~{E},13~{E},15~{E},17~{R},18~{S},20~{S})-20-[(1~{R})-1-[(2~{S},3~{R},4~{R},5~{S},6~{R})-5-[(2~{S},4~{S},5~{S},6~{R})-5-[(2~{S},4~{R},5~{R},6~{R})-4,6-dimethyl-4,5-bis(oxidanyl)oxan-2-yl]oxy-6-methyl-4-oxidanyl-oxan-2-yl]oxy-3-methoxy-6-(3-methoxypropyl)-5-methyl-2,4-bis(oxidanyl)oxan-2-yl]ethyl]-5,18-dimethoxy-3,7,9,11,13,15-hexamethyl-10-[(2~{R},3~{S},4~{R},5~{R},6~{S})-6-methyl-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-17-oxidanyl-1-oxacycloicosa-3,5,7,11,13,15-hexaen-2-one × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.10 Å
7MD3 The F1 region of apoptolidin-bound Saccharomyces cerevisiae ATP synthase Deposited 2021-04-03 Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 36–545（510 aa）
Chain B 36–545（510 aa）
Chain C 36–545（510 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 PO4 PHOSPHATE ION × 1 ZH7 (3~{E},5~{E},7~{E},9~{R},10~{R},11~{E},13~{E},17~{S},18~{S},20~{S})-18-methoxy-20-[(~{R})-[(2~{R},3~{R},4~{S},5~{R},6~{R})-6-[(2~{R})-3-methoxy-2-[(2~{R},4~{S},5~{S},6~{S})-5-[(2~{S},4~{R},5~{R},6~{R})-4-methoxy-6-methyl-5-oxidanyl-oxan-2-yl]oxy-4,6-dimethyl-4-oxidanyl-oxan-2-yl]oxy-propyl]-3,5-dimethyl-2,4-bis(oxidanyl)oxan-2-yl]-oxidanyl-methyl]-10-[(2~{R},3~{S},4~{S},5~{R},6~{S})-5-methoxy-6-methyl-3,4-bis(oxidanyl)oxan-2-yl]oxy-3,5,7,9,13-pentamethyl-17-oxidanyl-1-oxacycloicosa-3,5,7,11,13-pentaen-2-one × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.30 Å
7TJS Yeast ATP synthase F1 region State 1-3catalytic beta_tight closed without exogenous ATP Deposited 2022-01-17 Different construct Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain A 36–545（510 aa）
Chain B 36–545（510 aa）
Chain C 36–545（510 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 PO4 PHOSPHATE ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.20 Å
8FKJ Yeast ATP Synthase in conformation-3, at pH 6 Deposited 2022-12-21 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain A 39–545（507 aa）
Chain B 39–545（507 aa）
Chain C 39–545（507 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å
8FL8 Yeast ATP Synthase structure in presence of MgATP Deposited 2022-12-21 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain A 39–545（507 aa）
Chain B 39–545（507 aa）
Chain C 39–545（507 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q4L9_YEASX
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–485； UniProt 61–545 Author chain B； PDBConstruct 1–485； UniProt 61–545 Author chain C； PDBConstruct 1–485； UniProt 61–545

ATP synthase subunit beta

OrganismNot specified

UniProt A0A6A5PX46

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 × 7 PDB declaration: heptameric（7） Consistent with protein copy count Chain D； UniProt 41–509 Chain E； UniProt 41–509 Chain F； UniProt 41–509 Not recorded ATP synthase subunit alpha × 3 （A0A6A5Q4L9） ATP synthase subunit gamma × 1 （A0A6A5Q493） ATP ADENOSINE-5'-TRIPHOSPHATE × 5 MG MAGNESIUM ION × 5 XBC Cruentaren A × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE Resolution 2.90 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.

Other PDB Difference from Current Entry 8F2K Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7MD2 The F1 region of ammocidin-bound Saccharomyces cerevisiae ATP synthase Deposited 2021-04-03 Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain D 34–511（478 aa）
Chain E 34–511（478 aa）
Chain F 34–511（478 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 PO4 PHOSPHATE ION × 1 ZHD (3~{E},5~{Z},7~{E},9~{R},10~{S},11~{E},13~{E},15~{E},17~{R},18~{S},20~{S})-20-[(1~{R})-1-[(2~{S},3~{R},4~{R},5~{S},6~{R})-5-[(2~{S},4~{S},5~{S},6~{R})-5-[(2~{S},4~{R},5~{R},6~{R})-4,6-dimethyl-4,5-bis(oxidanyl)oxan-2-yl]oxy-6-methyl-4-oxidanyl-oxan-2-yl]oxy-3-methoxy-6-(3-methoxypropyl)-5-methyl-2,4-bis(oxidanyl)oxan-2-yl]ethyl]-5,18-dimethoxy-3,7,9,11,13,15-hexamethyl-10-[(2~{R},3~{S},4~{R},5~{R},6~{S})-6-methyl-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-17-oxidanyl-1-oxacycloicosa-3,5,7,11,13,15-hexaen-2-one × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.10 Å
7MD3 The F1 region of apoptolidin-bound Saccharomyces cerevisiae ATP synthase Deposited 2021-04-03 Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain D 34–511（478 aa）
Chain E 34–511（478 aa）
Chain F 34–511（478 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 PO4 PHOSPHATE ION × 1 ZH7 (3~{E},5~{E},7~{E},9~{R},10~{R},11~{E},13~{E},17~{S},18~{S},20~{S})-18-methoxy-20-[(~{R})-[(2~{R},3~{R},4~{S},5~{R},6~{R})-6-[(2~{R})-3-methoxy-2-[(2~{R},4~{S},5~{S},6~{S})-5-[(2~{S},4~{R},5~{R},6~{R})-4-methoxy-6-methyl-5-oxidanyl-oxan-2-yl]oxy-4,6-dimethyl-4-oxidanyl-oxan-2-yl]oxy-propyl]-3,5-dimethyl-2,4-bis(oxidanyl)oxan-2-yl]-oxidanyl-methyl]-10-[(2~{R},3~{S},4~{S},5~{R},6~{S})-5-methoxy-6-methyl-3,4-bis(oxidanyl)oxan-2-yl]oxy-3,5,7,9,13-pentamethyl-17-oxidanyl-1-oxacycloicosa-3,5,7,11,13-pentaen-2-one × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.30 Å
7TJS Yeast ATP synthase F1 region State 1-3catalytic beta_tight closed without exogenous ATP Deposited 2022-01-17 Different construct Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain D 34–511（478 aa）
Chain E 34–511（478 aa）
Chain F 34–511（478 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 PO4 PHOSPHATE ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.20 Å
8FKJ Yeast ATP Synthase in conformation-3, at pH 6 Deposited 2022-12-21 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain D 39–511（473 aa）
Chain E 39–511（473 aa）
Chain F 39–511（473 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å
8FL8 Yeast ATP Synthase structure in presence of MgATP Deposited 2022-12-21 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain D 39–511（473 aa）
Chain E 39–511（473 aa）
Chain F 39–511（473 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5PX46_YEASX
Isoform —
PDB entities 2
Chains and sequence ranges Author chain D； PDBConstruct 1–469； UniProt 41–509 Author chain E； PDBConstruct 1–469； UniProt 41–509 Author chain F； PDBConstruct 1–469； UniProt 41–509

ATP synthase subunit gamma

OrganismNot specified

UniProt A0A6A5Q493

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 × 7 PDB declaration: heptameric（7） Consistent with protein copy count Chain G； UniProt 34–308 Not recorded ATP synthase subunit alpha × 3 （A0A6A5Q4L9） ATP synthase subunit beta × 3 （A0A6A5PX46） ATP ADENOSINE-5'-TRIPHOSPHATE × 5 MG MAGNESIUM ION × 5 XBC Cruentaren A × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE Resolution 2.90 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.

Other PDB Difference from Current Entry 8F2K Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7MD2 The F1 region of ammocidin-bound Saccharomyces cerevisiae ATP synthase Deposited 2021-04-03 Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain G 34–311（278 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 PO4 PHOSPHATE ION × 1 ZHD (3~{E},5~{Z},7~{E},9~{R},10~{S},11~{E},13~{E},15~{E},17~{R},18~{S},20~{S})-20-[(1~{R})-1-[(2~{S},3~{R},4~{R},5~{S},6~{R})-5-[(2~{S},4~{S},5~{S},6~{R})-5-[(2~{S},4~{R},5~{R},6~{R})-4,6-dimethyl-4,5-bis(oxidanyl)oxan-2-yl]oxy-6-methyl-4-oxidanyl-oxan-2-yl]oxy-3-methoxy-6-(3-methoxypropyl)-5-methyl-2,4-bis(oxidanyl)oxan-2-yl]ethyl]-5,18-dimethoxy-3,7,9,11,13,15-hexamethyl-10-[(2~{R},3~{S},4~{R},5~{R},6~{S})-6-methyl-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-17-oxidanyl-1-oxacycloicosa-3,5,7,11,13,15-hexaen-2-one × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.10 Å
7MD3 The F1 region of apoptolidin-bound Saccharomyces cerevisiae ATP synthase Deposited 2021-04-03 Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain G 34–311（278 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 PO4 PHOSPHATE ION × 1 ZH7 (3~{E},5~{E},7~{E},9~{R},10~{R},11~{E},13~{E},17~{S},18~{S},20~{S})-18-methoxy-20-[(~{R})-[(2~{R},3~{R},4~{S},5~{R},6~{R})-6-[(2~{R})-3-methoxy-2-[(2~{R},4~{S},5~{S},6~{S})-5-[(2~{S},4~{R},5~{R},6~{R})-4-methoxy-6-methyl-5-oxidanyl-oxan-2-yl]oxy-4,6-dimethyl-4-oxidanyl-oxan-2-yl]oxy-propyl]-3,5-dimethyl-2,4-bis(oxidanyl)oxan-2-yl]-oxidanyl-methyl]-10-[(2~{R},3~{S},4~{S},5~{R},6~{S})-5-methoxy-6-methyl-3,4-bis(oxidanyl)oxan-2-yl]oxy-3,5,7,9,13-pentamethyl-17-oxidanyl-1-oxacycloicosa-3,5,7,11,13-pentaen-2-one × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.30 Å
7TJS Yeast ATP synthase F1 region State 1-3catalytic beta_tight closed without exogenous ATP Deposited 2022-01-17 Different construct Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain G 34–311（278 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 PO4 PHOSPHATE ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.20 Å
8FKJ Yeast ATP Synthase in conformation-3, at pH 6 Deposited 2022-12-21 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain G 38–307（270 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q493_YEASX
Isoform —
PDB entities 3
Chains and sequence ranges Author chain G； PDBConstruct 1–275； UniProt 34–308

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 8f2k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8f2k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8f2k
Deposition date deposition_date2022-11-08
Structure title titleStructure of yeast F1-ATPase determined with 100 micromolar cruentaren A
Keywords keywordsF1-ATPase, ATP Synthase, cruentaren A, drug development, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier42.05 Å
Radius of gyration Rg (electron density) rg_electron41.18 Å
Forward intensity I(0) i01430130000.00
Molecular weight molecular_weight318000.0 kDa
Excluded volume excluded_volume400750 ų
Envelope volume envelope_volume510960 ų
Hydration-shell volume shell_volume95783 ų
Envelope diameter envelope_diameter128.9 Å
Shell Rg shell_rg51.91 Å
Envelope Rg envelope_rg40.61 Å
Shape Rg shape_rg41.19 Å
Total Rg total_rg41.60 Å
Total atoms total_atoms22402
Residues n_residues2962
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax127.2 Å
Rg (real space) rg_real41.75 Å
Rg uncertainty (real space) rg_real_error0.55 Å
I(0) (real space) i0_real1.4300e+09
I(0) uncertainty (real space) i0_real_error2.0520e+07
Rg (reciprocal space) rg_reciprocal42.05 Å
I(0) (reciprocal space) i0_reciprocal1431000000.0000
Solution quality estimate total_estimate0.8956
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.5 Å
Skewness Skewness skewness0.030
Kurtosis Kurtosis kurtosis-0.560
Angular range angular_range— – 0.1900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha332000000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.952; Smooth: 0.937
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

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7. Fold Classification (SCOP + CATH) 18 domains

CATH v4.4 (18 domains)

Domain ID domain_id8f2kA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20 —
Domain ID domain_id8f2kA02
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_id8f2kA03
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_id8f2kB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20 —
Domain ID domain_id8f2kB02
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_id8f2kB03
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_id8f2kC01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20 —
Domain ID domain_id8f2kC02
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_id8f2kC03
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_id8f2kD01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170 —
Domain ID domain_id8f2kD02
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_id8f2kD03
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_id8f2kE01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170 —
Domain ID domain_id8f2kE02
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_id8f2kE03
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_id8f2kF01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170 —
Domain ID domain_id8f2kF02
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_id8f2kF03
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
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8. Citations (1)

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9. Files and Curves (10)