2c9v

Atomic resolution structure of Cu-Zn Human Superoxide dismutase

Method: X-RAY DIFFRACTION Dmax: 70.0 Å Quality: GOOD

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

SUPEROXIDE DISMUTASE [CU-ZN]

HOMO SAPIENS

UniProt P00441

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 1–153 Chain F; UniProt 1–153 Not recorded CU COPPER (II) ION × 2 ZN ZINC ION × 2 SO4 SULFATE ION × 5 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.75;3.0M AMMONIUM SULPHATE, 0.1M NACL, 50MM ACETATE BUFFER, pH 4.75 Resolution 1.07 Å R-free 0.158

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.

153 other PDB entries and 375 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SODC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–153; UniProt 1–153 Author chain F; PDBConstruct 1–153; UniProt 1–153

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 2c9v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2c9v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2c9v
Deposition date deposition_date2005-12-14
Structure title titleAtomic resolution structure of Cu-Zn Human Superoxide dismutase
Keywords keywords;OXIDOREDUCTASE, ACETYLATION, AMYOTROPHIC LATERAL SCLEROSIS, ANTIOXIDANT, COPPER, DISEASE MUTATION, HUMAN CU, METAL-BINDING, OXIOREDUCTASE, ZINC, ZN SUPEROXIDE DISMUTASE ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.08
Radius of gyration Rg (electron density) rg_electron20.08
Forward intensity I(0) i021639900.00
Molecular weight molecular_weight32381.0 kDa
Excluded volume excluded_volume39236 ų
Envelope volume envelope_volume46865 ų
Hydration-shell volume shell_volume19864 ų
Envelope diameter envelope_diameter72.5
Shell Rg shell_rg26.16
Envelope Rg envelope_rg20.35
Shape Rg shape_rg20.07
Total Rg total_rg20.86
Total atoms total_atoms2251
Residues n_residues306
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 dmax70.0
Rg (real space) rg_real21.08
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real2.1640e+07
I(0) uncertainty (real space) i0_real_error2.7110e+05
Rg (reciprocal space) rg_reciprocal21.08
I(0) (reciprocal space) i0_reciprocal21640000.0000
Solution quality estimate total_estimate0.8908
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.7
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.380
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2346000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2c9va_
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_idd2c9vf_
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_id2c9vA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id2c9vF00
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)