3gzp

HUMAN SOD1 G93A Metal-free Variant

Method: X-RAY DIFFRACTION Dmax: 82.6 Å Quality: EXCELLENT

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 2–154 Chain B; UniProt 2–154 Mutation:G93A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;2.4 M ammonium sulfate, 0.1 M HEPES, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.10 Å R-free 0.248
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 2–154 Chain D; UniProt 2–154 Mutation:G93A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;2.4 M ammonium sulfate, 0.1 M HEPES, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.10 Å R-free 0.248

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 374 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 2–154 Author chain B; PDBConstruct 1–153; UniProt 2–154 Author chain C; PDBConstruct 1–153; UniProt 2–154 Author chain D; PDBConstruct 1–153; UniProt 2–154

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 3gzp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3gzp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3gzp
Deposition date deposition_date2009-04-07
Structure title titleHUMAN SOD1 G93A Metal-free Variant
Keywords keywords;OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT, METAL-BINDING, COPPER, ZINC, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION, ACETYLATION, CYTOPLASM, APO, Disulfide bond, Phosphoprotein, Ubl conjugation ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.64
Radius of gyration Rg (electron density) rg_electron25.61
Forward intensity I(0) i060790100.00
Molecular weight molecular_weight57538.0 kDa
Excluded volume excluded_volume70786 ų
Envelope volume envelope_volume88505 ų
Hydration-shell volume shell_volume28606 ų
Envelope diameter envelope_diameter87.1
Shell Rg shell_rg33.10
Envelope Rg envelope_rg25.46
Shape Rg shape_rg25.61
Total Rg total_rg26.39
Total atoms total_atoms4044
Residues n_residues558
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 dmax82.6
Rg (real space) rg_real26.52
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real6.0790e+07
I(0) uncertainty (real space) i0_real_error8.4000e+05
Rg (reciprocal space) rg_reciprocal26.56
I(0) (reciprocal space) i0_reciprocal60790000.0000
Solution quality estimate total_estimate0.9087
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary81.2
Skewness Skewness skewness0.123
Kurtosis Kurtosis kurtosis-0.633
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8137000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.947

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3gzpa_
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_idd3gzpb_
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_idd3gzpc_
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_idd3gzpd_
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 (4 domains)

Domain ID domain_id3gzpA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id3gzpB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id3gzpC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id3gzpD00
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)