3zia

The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1

Method: X-RAY DIFFRACTION Dmax: 243.4 Å Quality: GOOD

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

ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL

OrganismNot specified

UniProt P07251

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain K; UniProt 36–545 Chain L; UniProt 36–545 Chain M; UniProt 36–545 Not recorded ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P21306) ATPASE INHIBITOR, MITOCHONDRIAL × 1 (P01097) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;296 K;ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O). Resolution 2.50 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 36–545 Chain B; UniProt 36–545 Chain C; UniProt 36–545 Not recorded ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P21306) ATPASE INHIBITOR, MITOCHONDRIAL × 1 (P01097) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;296 K;ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O). Resolution 2.50 Å R-free 0.262

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.

51 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPA_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–510; UniProt 36–545 Author chain B; PDBConstruct 1–510; UniProt 36–545 Author chain C; PDBConstruct 1–510; UniProt 36–545 Author chain K; PDBConstruct 1–510; UniProt 36–545 Author chain L; PDBConstruct 1–510; UniProt 36–545 Author chain M; PDBConstruct 1–510; UniProt 36–545

ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL

OrganismNot specified

UniProt P00830

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain N; UniProt 34–511 Chain O; UniProt 34–511 Chain P; UniProt 34–511 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P21306) ATPASE INHIBITOR, MITOCHONDRIAL × 1 (P01097) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;296 K;ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O). Resolution 2.50 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain D; UniProt 34–511 Chain E; UniProt 34–511 Chain F; UniProt 34–511 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P21306) ATPASE INHIBITOR, MITOCHONDRIAL × 1 (P01097) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;296 K;ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O). Resolution 2.50 Å R-free 0.262

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.

51 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPB_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–478; UniProt 34–511 Author chain E; PDBConstruct 1–478; UniProt 34–511 Author chain F; PDBConstruct 1–478; UniProt 34–511 Author chain N; PDBConstruct 1–478; UniProt 34–511 Author chain O; PDBConstruct 1–478; UniProt 34–511 Author chain P; PDBConstruct 1–478; UniProt 34–511

ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL

OrganismNot specified

UniProt P38077

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain Q; UniProt 34–311 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P21306) ATPASE INHIBITOR, MITOCHONDRIAL × 1 (P01097) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;296 K;ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O). Resolution 2.50 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain G; UniProt 34–311 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P21306) ATPASE INHIBITOR, MITOCHONDRIAL × 1 (P01097) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;296 K;ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O). Resolution 2.50 Å R-free 0.262

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.

52 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPG_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–278; UniProt 34–311 Author chain Q; PDBConstruct 1–278; UniProt 34–311

ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL

OrganismNot specified

UniProt Q12165

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain R; UniProt 23–160 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P21306) ATPASE INHIBITOR, MITOCHONDRIAL × 1 (P01097) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;296 K;ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O). Resolution 2.50 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain H; UniProt 23–160 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P21306) ATPASE INHIBITOR, MITOCHONDRIAL × 1 (P01097) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;296 K;ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O). Resolution 2.50 Å R-free 0.262

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.

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

View Construct and Data Evidence
UniProt name ATPD_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–138; UniProt 23–160 Author chain R; PDBConstruct 1–138; UniProt 23–160

ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL

OrganismNot specified

UniProt P21306

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain S; UniProt 2–62 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATPASE INHIBITOR, MITOCHONDRIAL × 1 (P01097) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;296 K;ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O). Resolution 2.50 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain I; UniProt 2–62 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATPASE INHIBITOR, MITOCHONDRIAL × 1 (P01097) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;296 K;ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O). Resolution 2.50 Å R-free 0.262

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.

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

View Construct and Data Evidence
UniProt name ATP5E_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–61; UniProt 2–62 Author chain S; PDBConstruct 1–61; UniProt 2–62

ATPASE INHIBITOR, MITOCHONDRIAL

SACCHAROMYCES CEREVISIAE

UniProt P01097

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain T; UniProt 23–85 Fragment:INHIBITOR PROTEIN, UNP RESIDUES 23-75 Mutation:YES ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P21306) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;296 K;ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O). Resolution 2.50 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain J; UniProt 23–85 Fragment:INHIBITOR PROTEIN, UNP RESIDUES 23-75 Mutation:YES ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P21306) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;296 K;ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O). Resolution 2.50 Å R-free 0.262

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name ATIF_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–63; UniProt 23–85 Author chain T; PDBConstruct 1–63; UniProt 23–85

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 3zia

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3zia
Deposition date deposition_date2013-01-07
Structure title titleThe structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1
Keywords keywordsHYDROLASE, NATURAL INHIBITOR, CATALYSIS, INTERMEDIATE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier69.27
Radius of gyration Rg (electron density) rg_electron69.55
Forward intensity I(0) i07182320000.00
Molecular weight molecular_weight725540.0 kDa
Excluded volume excluded_volume912630 ų
Envelope volume envelope_volume1283900 ų
Hydration-shell volume shell_volume151910 ų
Envelope diameter envelope_diameter256.6
Shell Rg shell_rg68.58
Envelope Rg envelope_rg69.57
Shape Rg shape_rg69.55
Total Rg total_rg69.50
Total atoms total_atoms51090
Residues n_residues6676
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 dmax243.4
Rg (real space) rg_real69.53
Rg uncertainty (real space) rg_real_error2.70
I(0) (real space) i0_real7.1820e+09
I(0) uncertainty (real space) i0_real_error1.6140e+08
Rg (reciprocal space) rg_reciprocal68.29
I(0) (reciprocal space) i0_reciprocal7165000000.0000
Solution quality estimate total_estimate0.8118
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary63.5
Skewness Skewness skewness0.489
Kurtosis Kurtosis kurtosis-0.414
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1284000000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.649; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.651

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 86 domains

SCOP 2.08 (44 domains)

Domain ID domain_idd3ziaa1
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_idd3ziaa2
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_idd3ziaa3
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_idd3ziab1
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_idd3ziab2
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_idd3ziab3
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_idd3ziac1
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_idd3ziac2
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_idd3ziac3
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_idd3ziad1
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_idd3ziad2
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_idd3ziad3
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_idd3ziae1
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_idd3ziae2
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_idd3ziae3
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_idd3ziaf1
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_idd3ziaf2
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_idd3ziaf3
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_idd3ziag_
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_idd3ziah1
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_idd3ziah2
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.10 — Epsilon subunit of F1F0-ATP synthase C-terminal domain
Family Family familya.2.10.1 — Epsilon subunit of F1F0-ATP synthase C-terminal domain
Domain ID domain_idd3ziai_
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
Domain ID domain_idd3ziak1
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_idd3ziak2
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_idd3ziak3
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_idd3zial1
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_idd3zial2
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_idd3zial3
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_idd3ziam1
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_idd3ziam2
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_idd3ziam3
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_idd3zian1
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_idd3zian2
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_idd3zian3
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_idd3ziao1
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_idd3ziao2
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_idd3ziao3
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_idd3ziap1
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_idd3ziap2
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_idd3ziap3
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_idd3ziaq_
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_idd3ziar1
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_idd3ziar2
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.10 — Epsilon subunit of F1F0-ATP synthase C-terminal domain
Family Family familya.2.10.1 — Epsilon subunit of F1F0-ATP synthase C-terminal domain
Domain ID domain_idd3zias_
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 (42 domains)

Domain ID domain_id3ziaA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id3ziaA02
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_id3ziaA03
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_id3ziaB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id3ziaB02
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_id3ziaB03
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_id3ziaC01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id3ziaC02
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_id3ziaC03
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_id3ziaD01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id3ziaD02
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_id3ziaD03
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_id3ziaE01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id3ziaE02
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_id3ziaE03
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_id3ziaF01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id3ziaF02
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_id3ziaF03
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_id3ziaG01
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_id3ziaG02
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_id3ziaI00
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_id3ziaK01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id3ziaK02
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_id3ziaK03
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_id3ziaL01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id3ziaL02
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_id3ziaL03
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_id3ziaM01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id3ziaM02
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_id3ziaM03
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_id3ziaN01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id3ziaN02
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_id3ziaN03
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_id3ziaO01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id3ziaO02
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_id3ziaO03
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_id3ziaP01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id3ziaP02
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_id3ziaP03
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_id3ziaQ01
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_id3ziaQ02
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_id3ziaS00
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

8. Citations (1)

9. Files and Curves (10)