2jmx

OSCP-NT (1-120) in complex with N-terminal (1-25) alpha subunit from F1-ATPase

Method: SOLUTION NMR Dmax: 45.7 Å Quality: REASONABLE

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

ATP synthase O subunit, 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 24–143 Fragment:ATP synthase O subunit, residues 1-120 ATP synthase subunit alpha heart isoform, mitochondrial × 1 (P19483) SOLUTION NMR NMR measurement conditions:pH 6.5;300 K;Ionic strength (raw mmCIF value) 0.5;Pressure ambient NMR sample composition:0.5 mM [U-99% 13C, U-99% 15N] oscp-nt, 1.5 mM alpha-nt, 20 mM sodium phosphate, pH 6.5, 0.5 M NaCl, 0.001% PMSF 95% H2O, 5% D2O | 95% H2O/5% D2O 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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPO_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–120; UniProt 24–143

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 44–68 Fragment:ATP synthase subunit alpha heart isoform, residues 1-25 ATP synthase O subunit, mitochondrial × 1 (P13621) SOLUTION NMR NMR measurement conditions:pH 6.5;300 K;Ionic strength (raw mmCIF value) 0.5;Pressure ambient NMR sample composition:0.5 mM [U-99% 13C, U-99% 15N] oscp-nt, 1.5 mM alpha-nt, 20 mM sodium phosphate, pH 6.5, 0.5 M NaCl, 0.001% PMSF 95% H2O, 5% D2O | 95% H2O/5% D2O 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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–25; UniProt 44–68

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 2jmx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2jmx
Deposition date deposition_date2006-12-12
Structure title titleOSCP-NT (1-120) in complex with N-terminal (1-25) alpha subunit from F1-ATPase
Keywords keywordsoscp-nt alpha-nt complex, HYDROLASE; HYDROLASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.26
Radius of gyration Rg (electron density) rg_electron17.37
Forward intensity I(0) i02973870000.00
Molecular weight molecular_weight475820.0 kDa
Excluded volume excluded_volume602980 ų
Envelope volume envelope_volume95061 ų
Hydration-shell volume shell_volume30972 ų
Envelope diameter envelope_diameter86.7
Shell Rg shell_rg33.01
Envelope Rg envelope_rg25.91
Shape Rg shape_rg17.34
Total Rg total_rg17.78
Total atoms total_atoms68490
Residues n_residues4350
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 dmax45.7
Rg (real space) rg_real16.32
Rg uncertainty (real space) rg_real_error0.07
I(0) (real space) i0_real2.8290e+09
I(0) uncertainty (real space) i0_real_error2.5400e+07
Rg (reciprocal space) rg_reciprocal17.33
I(0) (reciprocal space) i0_reciprocal2974000000.0000
Solution quality estimate total_estimate0.6826
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary19.2
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.350
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha3.9570
Highest regularization parameter α highest_alpha511400.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.981; Stabil: 0.978; Sysdev: 0.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2jmxA01
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)