2odx

Solution structure of Zn(II)Cox4

Method: SOLUTION NMR Dmax: 35.2 Å Quality: EXCELLENT

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

Cytochrome c oxidase polypeptide IV

Saccharomyces cerevisiae

UniProt P04037

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 79–155 Fragment:Cox4 subunit ZN ZINC ION × 1 SOLUTION NMR NMR measurement conditions:pH 6.9;298 K;Ionic strength (raw mmCIF value) 50 mM phosphate, 200 mM NaCl;Pressure 1 NMR sample composition:1 mM Zn(II)Cox4 U-15N, 50mM phosphate buffer NA, 200 mM NaCl, 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM Zn(II)Cox4 U-15N,13C, 50mM phosphate buffer NA, 200 mM NaCl, 90% H2O, 10% D2O | 90% H2O/10% 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.

12 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–80; UniProt 79–155

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 2odx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2odx
Deposition date deposition_date2006-12-27
Structure title titleSolution structure of Zn(II)Cox4
Keywords keywordsALL BETA-PROTEIN, METALLO-PROTEIN, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier10.82
Radius of gyration Rg (electron density) rg_electron10.89
Forward intensity I(0) i0238146000.00
Molecular weight molecular_weight128090.0 kDa
Excluded volume excluded_volume158750 ų
Envelope volume envelope_volume11555 ų
Hydration-shell volume shell_volume8698 ų
Envelope diameter envelope_diameter37.7
Shell Rg shell_rg16.92
Envelope Rg envelope_rg11.94
Shape Rg shape_rg10.91
Total Rg total_rg10.93
Total atoms total_atoms17388
Residues n_residues1134
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 dmax35.2
Rg (real space) rg_real10.82
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.3810e+08
I(0) uncertainty (real space) i0_real_error2.6570e+06
Rg (reciprocal space) rg_reciprocal10.82
I(0) (reciprocal space) i0_reciprocal238100000.0000
Solution quality estimate total_estimate0.9026
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.3
Skewness Skewness skewness0.189
Kurtosis Kurtosis kurtosis-0.692
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28490.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.914; Smooth: 0.961

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_id2odxA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology260 — HSP40/DNAj peptide-binding domain
Homologous superfamily homologous superfamily40 — q5lls5 like domains

8. Citations (1)

9. Files and Curves (10)