1q0e

Atomic resolution (1.15 ) crystal structure of bovine copper, zinc superoxide dismutase

Method: X-RAY DIFFRACTION Dmax: 71.8 Å Quality: GOOD

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

Superoxide dismutase [Cu-Zn]

OrganismNot specified

UniProt P00442

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 1–151 Fragment:Copper, Zinc Superoxide Dismutase Non-standard monomer:Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;15 % PEG-4000, 50 mM glycyl-glycine , 100 mM NaCl, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.15 Å R-free 0.166
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–151 Fragment:Copper, Zinc Superoxide Dismutase Non-standard monomer:Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;15 % PEG-4000, 50 mM glycyl-glycine , 100 mM NaCl, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.15 Å R-free 0.166

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.

24 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SODC_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–152; UniProt 1–151 Author chain B; PDBConstruct 2–152; UniProt 1–151

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 1q0e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1q0e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1q0e
Deposition date deposition_date2003-07-16
Structure title titleAtomic resolution (1.15 ) crystal structure of bovine copper, zinc superoxide dismutase
Keywords keywordsbovine, superoxide dismutase, atomic resolution, copper, zinc, OXIDOREDUCTASE, METAL BINDING PROTEIN; OXIDOREDUCTASE, METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.18
Radius of gyration Rg (electron density) rg_electron20.23
Forward intensity I(0) i019638400.00
Molecular weight molecular_weight31394.0 kDa
Excluded volume excluded_volume38418 ų
Envelope volume envelope_volume46780 ų
Hydration-shell volume shell_volume19823 ų
Envelope diameter envelope_diameter73.3
Shell Rg shell_rg26.17
Envelope Rg envelope_rg20.50
Shape Rg shape_rg20.25
Total Rg total_rg20.98
Total atoms total_atoms2191
Residues n_residues302
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 dmax71.8
Rg (real space) rg_real21.21
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.9640e+07
I(0) uncertainty (real space) i0_real_error2.5160e+05
Rg (reciprocal space) rg_reciprocal21.21
I(0) (reciprocal space) i0_reciprocal19640000.0000
Solution quality estimate total_estimate0.8720
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.2
Skewness Skewness skewness0.388
Kurtosis Kurtosis kurtosis-0.355
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3121000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.814; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1q0ea_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.8 — Cu,Zn superoxide dismutase-like
Family Family familyb.1.8.1 — Cu,Zn superoxide dismutase-like
Domain ID domain_idd1q0eb_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.8 — Cu,Zn superoxide dismutase-like
Family Family familyb.1.8.1 — Cu,Zn superoxide dismutase-like

CATH v4.4 (2 domains)

Domain ID domain_id1q0eA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id1q0eB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain

8. Citations (1)

9. Files and Curves (10)