2wss

The structure of the membrane extrinsic region of bovine ATP synthase

Method: X-RAY DIFFRACTION Dmax: 260.8 Å Quality: GOOD

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

ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL

OrganismNot specified

UniProt P19483

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain A; UniProt 44–553 Chain B; UniProt 44–553 Chain C; UniProt 44–553 Not recorded ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain J; UniProt 44–553 Chain K; UniProt 44–553 Chain L; UniProt 44–553 Not recorded ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271

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 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPA_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–510; UniProt 44–553 Author chain B; PDBConstruct 1–510; UniProt 44–553 Author chain C; PDBConstruct 1–510; UniProt 44–553 Author chain J; PDBConstruct 1–510; UniProt 44–553 Author chain K; PDBConstruct 1–510; UniProt 44–553 Author chain L; PDBConstruct 1–510; UniProt 44–553

ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL

OrganismNot specified

UniProt P00829

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain D; UniProt 47–528 Chain E; UniProt 47–528 Chain F; UniProt 47–528 Fragment:RESIDUES 47-528 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain M; UniProt 47–528 Chain N; UniProt 47–528 Chain O; UniProt 47–528 Fragment:RESIDUES 47-528 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271

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 58 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 Author chain M; PDBConstruct 1–482; UniProt 47–528 Author chain N; PDBConstruct 1–482; UniProt 47–528 Author chain O; PDBConstruct 1–482; UniProt 47–528

ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL

OrganismNot specified

UniProt P05631

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain G; UniProt 26–297 Fragment:HEART ISOFORM, RESIDUES 26-297 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain P; UniProt 26–297 Fragment:HEART ISOFORM, RESIDUES 26-297 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271

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 61 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 Author chain P; PDBConstruct 1–272; UniProt 26–297

ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL

OrganismNot specified

UniProt P05630

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain H; UniProt 23–168 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain Q; UniProt 23–168 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271

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 38 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 Author chain Q; PDBConstruct 1–146; UniProt 23–168

ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL

OrganismNot specified

UniProt P05632

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain I; UniProt 2–51 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain R; UniProt 2–51 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271

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 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP5E_BOVIN
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–50; UniProt 2–51 Author chain R; PDBConstruct 1–50; UniProt 2–51

ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL

BOS TAURUS

UniProt P13621

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain S; UniProt 24–213 Non-standard monomer:Yes (specific site not provided by mmCIF) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain W; UniProt 24–213 Non-standard monomer:Yes (specific site not provided by mmCIF) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271

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.

30 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPO_BOVIN
Isoform
PDB entities 6
Chains and sequence ranges Author chain S; PDBConstruct 1–190; UniProt 24–213 Author chain W; PDBConstruct 1–190; UniProt 24–213

ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL

BOS TAURUS

UniProt P13619

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain T; UniProt 141–256 Fragment:RESIDUES 141-256 Non-standard monomer:Yes (specific site not provided by mmCIF) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain X; UniProt 141–256 Fragment:RESIDUES 141-256 Non-standard monomer:Yes (specific site not provided by mmCIF) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271

Other States of the Same Protein in the Database

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

31 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AT5F1_BOVIN
Isoform
PDB entities 7
Chains and sequence ranges Author chain T; PDBConstruct 1–116; UniProt 141–256 Author chain X; PDBConstruct 1–116; UniProt 141–256

ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL

BOS TAURUS

UniProt P13620

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain U; UniProt 2–119 Fragment:RESIDUES 2-119 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271

Other States of the Same Protein in the Database

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

29 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP5H_BOVIN
Isoform
PDB entities 8
Chains and sequence ranges Author chain U; PDBConstruct 1–118; UniProt 2–119

ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL

BOS TAURUS

UniProt P02721

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain V; UniProt 33–108 Non-standard monomer:Yes (specific site not provided by mmCIF) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain Z; UniProt 33–108 Non-standard monomer:Yes (specific site not provided by mmCIF) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (P05630) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 (P05632) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 1 (P13619) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;MICROBATCH UNDER OIL Resolution 3.20 Å R-free 0.271

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.

30 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP5J_BOVIN
Isoform
PDB entities 9
Chains and sequence ranges Author chain V; PDBConstruct 1–76; UniProt 33–108 Author chain Z; PDBConstruct 1–76; UniProt 33–108

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 2wss

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2wss
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2wss
Deposition date deposition_date2009-09-09
Structure title titleThe structure of the membrane extrinsic region of bovine ATP synthase
Keywords keywords;HYDROGEN ION TRANSPORT, ATP SYNTHESIS, PHOSPHOPROTEIN, UBL CONJUGATION, TRANSIT PEPTIDE, NUCLEOTIDE-BINDING, ACETYLATION, ATP-BINDING, ION TRANSPORT, MITOCHONDRION, PYRROLIDONE CARBOXYLIC ACID, HYDROLASE, TRANSPORT ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier72.63
Radius of gyration Rg (electron density) rg_electron72.69
Forward intensity I(0) i08384130000.00
Molecular weight molecular_weight783010.0 kDa
Excluded volume excluded_volume983670 ų
Envelope volume envelope_volume1459400 ų
Hydration-shell volume shell_volume160860 ų
Envelope diameter envelope_diameter247.1
Shell Rg shell_rg73.87
Envelope Rg envelope_rg72.72
Shape Rg shape_rg72.69
Total Rg total_rg72.71
Total atoms total_atoms54945
Residues n_residues7128
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 dmax260.8
Rg (real space) rg_real76.75
Rg uncertainty (real space) rg_real_error1.43
I(0) (real space) i0_real8.4270e+09
I(0) uncertainty (real space) i0_real_error1.6660e+08
Rg (reciprocal space) rg_reciprocal71.82
I(0) (reciprocal space) i0_reciprocal8367000000.0000
Solution quality estimate total_estimate0.8507
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary71.1
Skewness Skewness skewness0.520
Kurtosis Kurtosis kurtosis-0.325
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha1.3150
Highest regularization parameter α highest_alpha2031000000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.670; Stabil: 0.864; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.487

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

7. Fold Classification (SCOP + CATH) 50 domains

CATH v4.4 (50 domains)

Domain ID domain_id2wssA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id2wssA02
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_id2wssA03
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_id2wssB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id2wssB02
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_id2wssB03
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_id2wssC01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id2wssC02
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_id2wssC03
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_id2wssD01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id2wssD02
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_id2wssD03
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_id2wssE01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id2wssE02
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_id2wssE03
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_id2wssF01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id2wssF02
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_id2wssF03
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_id2wssG01
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_id2wssG02
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_id2wssH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology15 — ATP Synthase; domain 1
Homologous superfamily homologous superfamily10 — F0F1 ATP synthase delta/epsilon subunit, N-terminal
Domain ID domain_id2wssH02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily440 — ATP synthase delta/epsilon subunit, C-terminal domain
Domain ID domain_id2wssI00
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_id2wssJ01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id2wssJ02
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_id2wssJ03
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_id2wssK01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id2wssK02
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_id2wssK03
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_id2wssL01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id2wssL02
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_id2wssL03
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_id2wssM01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id2wssM02
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_id2wssM03
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_id2wssN01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id2wssN02
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_id2wssN03
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_id2wssO01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id2wssO02
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_id2wssO03
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_id2wssP01
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_id2wssP02
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_id2wssQ01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology15 — ATP Synthase; domain 1
Homologous superfamily homologous superfamily10 — F0F1 ATP synthase delta/epsilon subunit, N-terminal
Domain ID domain_id2wssQ02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily440 — ATP synthase delta/epsilon subunit, C-terminal domain
Domain ID domain_id2wssR00
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_id2wssS01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily20 — N-terminal domain of the delta subunit of the F1F0-ATP synthase
Domain ID domain_id2wssT00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily2210
Domain ID domain_id2wssV01
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology280 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily200
Domain ID domain_id2wssW01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily20 — N-terminal domain of the delta subunit of the F1F0-ATP synthase

8. Citations (1)

9. Files and Curves (10)