2z7u

Crystal Structure of H2O2 treated Cu,Zn-SOD

Method: X-RAY DIFFRACTION Dmax: 70.8 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–152 Chain B; UniProt 2–152 Not recorded ZN ZINC ION × 2 CU COPPER (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.4;295 K;20% (w/v) PEG 4000, 20% (w/v) iso-propanol, 0.09M MES, 1mM EDTA, pH 6.4-6.7, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.10 Å R-free 0.238

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 38 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 1–151; UniProt 2–152 Author chain B; PDBConstruct 1–151; UniProt 2–152

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 2z7u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2z7u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2z7u
Deposition date deposition_date2007-08-28
Structure title titleCrystal Structure of H2O2 treated Cu,Zn-SOD
Keywords keywordsmetalloprotein, dismutase, Acetylation, Antioxidant, Copper, Cytoplasm, Metal-binding, Oxidoreductase, Zinc; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.88
Radius of gyration Rg (electron density) rg_electron19.92
Forward intensity I(0) i019595400.00
Molecular weight molecular_weight31351.0 kDa
Excluded volume excluded_volume38361 ų
Envelope volume envelope_volume45142 ų
Hydration-shell volume shell_volume19438 ų
Envelope diameter envelope_diameter71.7
Shell Rg shell_rg25.96
Envelope Rg envelope_rg20.18
Shape Rg shape_rg19.94
Total Rg total_rg20.69
Total atoms total_atoms2188
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 dmax70.8
Rg (real space) rg_real20.91
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real1.9600e+07
I(0) uncertainty (real space) i0_real_error2.4510e+05
Rg (reciprocal space) rg_reciprocal20.91
I(0) (reciprocal space) i0_reciprocal19600000.0000
Solution quality estimate total_estimate0.8756
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.390
Kurtosis Kurtosis kurtosis-0.347
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2812000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.815; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.981

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_idd2z7ua_
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_idd2z7ub_
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_id2z7uA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id2z7uB00
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)