1vzs

Solution structure of subunit F6 from the peripheral stalk region of ATP synthase from bovine heart mitochondria

Method: SOLUTION NMR Dmax: 57.5 Å Quality: REASONABLE

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

ATP SYNTHASE COUPLING FACTOR 6, MITOCHONDRIAL PRECURSOR

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 33–108 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;300 K;Pressure 1 NMR sample composition:95% H2O, 5% D2O, 50MM NACL, 20 MM PHOSPHATE Resolution not provided

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 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPR_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; 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 1vzs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1vzs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1vzs
Deposition date deposition_date2004-05-25
Structure title titleSolution structure of subunit F6 from the peripheral stalk region of ATP synthase from bovine heart mitochondria
Keywords keywordsSYNTHASE, ATP SYNTHASE, PERIPHERAL STALK, F6 SUBUNIT, HYDROGEN ION TRANSPORT; SYNTHASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.06
Radius of gyration Rg (electron density) rg_electron14.57
Forward intensity I(0) i01286140000.00
Molecular weight molecular_weight304540.0 kDa
Excluded volume excluded_volume381080 ų
Envelope volume envelope_volume57194 ų
Hydration-shell volume shell_volume22850 ų
Envelope diameter envelope_diameter66.6
Shell Rg shell_rg27.73
Envelope Rg envelope_rg21.15
Shape Rg shape_rg14.53
Total Rg total_rg14.98
Total atoms total_atoms42500
Residues n_residues2584
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 dmax57.5
Rg (real space) rg_real15.12
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real1.2860e+09
I(0) uncertainty (real space) i0_real_error1.5920e+07
Rg (reciprocal space) rg_reciprocal15.11
I(0) (reciprocal space) i0_reciprocal1286000000.0000
Solution quality estimate total_estimate0.7264
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.0
Skewness Skewness skewness0.437
Kurtosis Kurtosis kurtosis-0.038
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha257900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.587; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.678; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1vzsa_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.45 — Mitochondrial ATP synthase coupling factor 6
Superfamily Superfamily superfamilyf.45.1 — Mitochondrial ATP synthase coupling factor 6
Family Family familyf.45.1.1 — Mitochondrial ATP synthase coupling factor 6

CATH v4.4 (1 domains)

Domain ID domain_id1vzsA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily110 — Mitochondrial ATP synthase-coupling factor 6

8. Citations (1)

9. Files and Curves (10)