2w6g

Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 3.

Method: X-RAY DIFFRACTION Dmax: 127.0 Å Quality: GOOD

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

ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, 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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–553 Chain B; UniProt 1–553 Chain C; UniProt 1–553 Not recorded ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;50 MM TRIS-HCL PH 8.2, 200 MM NACL, 20 MM MGSO4, 1 MM ADP, 1 MM ALCL3, 6 MM NAF 0.004% (W/V)PHENYLMETHYLSULFONYL FLUORIDE AND 12% (W/V) POLYETHYLENE GLYCOL 6000 Resolution 6.00 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name ATPA1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–553; UniProt 1–553 Author chain B; PDBConstruct 1–553; UniProt 1–553 Author chain C; PDBConstruct 1–553; UniProt 1–553

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain D; UniProt 1–528 Chain E; UniProt 1–528 Chain F; UniProt 1–528 Not recorded ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P05631) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;50 MM TRIS-HCL PH 8.2, 200 MM NACL, 20 MM MGSO4, 1 MM ADP, 1 MM ALCL3, 6 MM NAF 0.004% (W/V)PHENYLMETHYLSULFONYL FLUORIDE AND 12% (W/V) POLYETHYLENE GLYCOL 6000 Resolution 6.00 Å

Other States of the Same Protein in the Database

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

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

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain G; UniProt 1–298 Not recorded ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL × 3 (P19483) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00829) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;50 MM TRIS-HCL PH 8.2, 200 MM NACL, 20 MM MGSO4, 1 MM ADP, 1 MM ALCL3, 6 MM NAF 0.004% (W/V)PHENYLMETHYLSULFONYL FLUORIDE AND 12% (W/V) POLYETHYLENE GLYCOL 6000 Resolution 6.00 Å

Other States of the Same Protein in the Database

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

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 1–298; UniProt 1–298

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 2w6g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2w6g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2w6g
Deposition date deposition_date2008-12-18
Structure title titleLow resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 3.
Keywords keywords;ATP PHOSPHORYLASE (H+ TRANSPORTING), TRANSIT PEPTIDE, F1FO ATP PHOSPHORYLASE, ION TRANSPORT, MITOCHONDRION, ATP SYNTHESIS, CF(1), P-LOOP, HYDROLASE, NUCLEOTIDE-BINDING, HYDROGEN ION TRANSPORT, PYRROLIDONE CARBOXYLIC ACID, ATP-BINDING ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.35
Radius of gyration Rg (electron density) rg_electron41.42
Forward intensity I(0) i01487620000.00
Molecular weight molecular_weight324140.0 kDa
Excluded volume excluded_volume408390 ų
Envelope volume envelope_volume523800 ų
Hydration-shell volume shell_volume97515 ų
Envelope diameter envelope_diameter142.5
Shell Rg shell_rg52.18
Envelope Rg envelope_rg40.96
Shape Rg shape_rg41.42
Total Rg total_rg41.85
Total atoms total_atoms22795
Residues n_residues2997
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 dmax127.0
Rg (real space) rg_real42.03
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real1.4880e+09
I(0) uncertainty (real space) i0_real_error2.6540e+07
Rg (reciprocal space) rg_reciprocal42.34
I(0) (reciprocal space) i0_reciprocal1488000000.0000
Solution quality estimate total_estimate0.8950
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary54.9
Skewness Skewness skewness0.023
Kurtosis Kurtosis kurtosis-0.544
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha314400000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)