3h2p

Human SOD1 D124V Variant

Method: X-RAY DIFFRACTION Dmax: 62.8 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 2–154 Chain B; UniProt 2–154 Mutation:D124V ZN ZINC ION × 3 MLI MALONATE ION × 2 ACE ACETYL GROUP × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;2.4 M sodium malonate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.55 Å R-free 0.202

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 2–154 Author chain B; 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 3h2p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3h2p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3h2p
Deposition date deposition_date2009-04-14
Structure title titleHuman SOD1 D124V Variant
Keywords keywords;oxidoreductase, human cu, zn superoxide dismutase, antioxidant, metal-binding, copper, zinc, amyotrophic lateral sclerosis, disease mutation, Acetylation, Cytoplasm, 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_guinier19.17
Radius of gyration Rg (electron density) rg_electron18.15
Forward intensity I(0) i014018800.00
Molecular weight molecular_weight26682.0 kDa
Excluded volume excluded_volume32799 ų
Envelope volume envelope_volume38342 ų
Hydration-shell volume shell_volume17855 ų
Envelope diameter envelope_diameter63.4
Shell Rg shell_rg24.34
Envelope Rg envelope_rg18.45
Shape Rg shape_rg18.16
Total Rg total_rg19.02
Total atoms total_atoms1864
Residues n_residues255
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 dmax62.8
Rg (real space) rg_real19.11
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.4020e+07
I(0) uncertainty (real space) i0_real_error1.8090e+05
Rg (reciprocal space) rg_reciprocal19.12
I(0) (reciprocal space) i0_reciprocal14020000.0000
Solution quality estimate total_estimate0.8877
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.263
Kurtosis Kurtosis kurtosis-0.369
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2108000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.948

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3h2pa_
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_idd3h2pb_
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_id3h2pA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id3h2pB00
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)