4z1m

Bovine F1-ATPase inhibited by three copies of the inhibitor protein IF1 crystallised in the presence of thiophosphate.

Method: X-RAY DIFFRACTION Dmax: 129.4 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 × 10 PDB declaration: decameric(10) 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) ATPase inhibitor, mitochondrial × 3 (P01096) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 GOL GLYCEROL × 2 CL CHLORIDE ION × 11 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;295 K;Tris.HCl, MgCl2, EDTA, sodium monothiophosphate, ATP NaCl, spermidine, PEG 4000 Resolution 3.30 Å R-free 0.275

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name ATPA_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–510; UniProt 44–553 Author chain B; PDBConstruct 1–510; UniProt 44–553 Author chain C; 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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain D; UniProt 47–528 Chain E; UniProt 47–528 Chain F; UniProt 47–528 Not recorded ATP synthase subunit alpha, mitochondrial × 3 (P19483) ATP synthase subunit gamma, mitochondrial × 1 (P05631) ATPase inhibitor, mitochondrial × 3 (P01096) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 GOL GLYCEROL × 2 CL CHLORIDE ION × 11 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;295 K;Tris.HCl, MgCl2, EDTA, sodium monothiophosphate, ATP NaCl, spermidine, PEG 4000 Resolution 3.30 Å R-free 0.275

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name ATPB_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–482; UniProt 47–528 Author chain E; PDBConstruct 1–482; UniProt 47–528 Author chain F; PDBConstruct 1–482; UniProt 47–528

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain G; UniProt 26–298 Not recorded ATP synthase subunit alpha, mitochondrial × 3 (P19483) ATP synthase subunit beta, mitochondrial × 3 (P00829) ATPase inhibitor, mitochondrial × 3 (P01096) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 GOL GLYCEROL × 2 CL CHLORIDE ION × 11 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;295 K;Tris.HCl, MgCl2, EDTA, sodium monothiophosphate, ATP NaCl, spermidine, PEG 4000 Resolution 3.30 Å R-free 0.275

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name ATPG_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–273; UniProt 26–298

ATPase inhibitor, mitochondrial

Bos taurus

UniProt P01096

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 H; UniProt 26–85 Chain I; UniProt 26–85 Chain J; UniProt 26–85 Mutation:K39A ATP synthase subunit alpha, mitochondrial × 3 (P19483) ATP synthase subunit beta, mitochondrial × 3 (P00829) ATP synthase subunit gamma, mitochondrial × 1 (P05631) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 GOL GLYCEROL × 2 CL CHLORIDE ION × 11 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;295 K;Tris.HCl, MgCl2, EDTA, sodium monothiophosphate, ATP NaCl, spermidine, PEG 4000 Resolution 3.30 Å R-free 0.275

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.

23 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATIF1_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–60; UniProt 26–85 Author chain I; PDBConstruct 1–60; UniProt 26–85 Author chain J; PDBConstruct 1–60; UniProt 26–85

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 4z1m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4z1m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4z1m
Deposition date deposition_date2015-03-27
Structure title titleBovine F1-ATPase inhibited by three copies of the inhibitor protein IF1 crystallised in the presence of thiophosphate.
Keywords keywordsHydrolase, inhibitor protein; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.80
Radius of gyration Rg (electron density) rg_electron41.95
Forward intensity I(0) i01713680000.00
Molecular weight molecular_weight344160.0 kDa
Excluded volume excluded_volume431720 ų
Envelope volume envelope_volume564780 ų
Hydration-shell volume shell_volume102740 ų
Envelope diameter envelope_diameter147.4
Shell Rg shell_rg53.46
Envelope Rg envelope_rg41.73
Shape Rg shape_rg41.97
Total Rg total_rg42.33
Total atoms total_atoms24168
Residues n_residues3143
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 dmax129.4
Rg (real space) rg_real42.47
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real1.7140e+09
I(0) uncertainty (real space) i0_real_error3.0420e+07
Rg (reciprocal space) rg_reciprocal42.80
I(0) (reciprocal space) i0_reciprocal1714000000.0000
Solution quality estimate total_estimate0.8929
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary56.0
Skewness Skewness skewness0.024
Kurtosis Kurtosis kurtosis-0.542
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha481400000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.944; Smooth: 0.946

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 21 domains

CATH v4.4 (21 domains)

Domain ID domain_id4z1mA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id4z1mA02
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_id4z1mA03
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_id4z1mB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id4z1mB02
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_id4z1mB03
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_id4z1mC01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily20
Domain ID domain_id4z1mC02
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_id4z1mC03
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_id4z1mD01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id4z1mD02
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_id4z1mD03
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_id4z1mE01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id4z1mE02
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_id4z1mE03
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_id4z1mF01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily170
Domain ID domain_id4z1mF02
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_id4z1mF03
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_id4z1mG01
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_id4z1mG02
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_id4z1mH00
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 superfamily500 — Single helix bin

8. Citations (1)

9. Files and Curves (10)