1uxm

A4V mutant of human SOD1

Method: X-RAY DIFFRACTION Dmax: 164.1 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 B; UniProt 1–153 Mutation:YES CU COPPER (II) ION × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;0.2 M CA ACET, 15% PEG 2000, 0.1 M TRIS PH 8.0 Resolution 1.90 Å R-free 0.250
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–153 Chain D; UniProt 1–153 Mutation:YES CU COPPER (II) ION × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;0.2 M CA ACET, 15% PEG 2000, 0.1 M TRIS PH 8.0 Resolution 1.90 Å R-free 0.250
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–153 Chain F; UniProt 1–153 Mutation:YES CU COPPER (II) ION × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;0.2 M CA ACET, 15% PEG 2000, 0.1 M TRIS PH 8.0 Resolution 1.90 Å R-free 0.250
4 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–153 Chain H; UniProt 1–153 Mutation:YES CU COPPER (II) ION × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;0.2 M CA ACET, 15% PEG 2000, 0.1 M TRIS PH 8.0 Resolution 1.90 Å R-free 0.250
5 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 1–153 Chain J; UniProt 1–153 Mutation:YES CU COPPER (II) ION × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;0.2 M CA ACET, 15% PEG 2000, 0.1 M TRIS PH 8.0 Resolution 1.90 Å R-free 0.250
6 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain K; UniProt 1–153 Chain L; UniProt 1–153 Mutation:YES CU COPPER (II) ION × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;0.2 M CA ACET, 15% PEG 2000, 0.1 M TRIS PH 8.0 Resolution 1.90 Å R-free 0.250

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 370 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 B; PDBConstruct 1–153; UniProt 1–153 Author chain C; PDBConstruct 1–153; UniProt 1–153 Author chain D; PDBConstruct 1–153; UniProt 1–153 Author chain E; PDBConstruct 1–153; UniProt 1–153 Author chain F; PDBConstruct 1–153; UniProt 1–153 Author chain G; PDBConstruct 1–153; UniProt 1–153 Author chain H; PDBConstruct 1–153; UniProt 1–153 Author chain I; PDBConstruct 1–153; UniProt 1–153 Author chain J; PDBConstruct 1–153; UniProt 1–153 Author chain K; PDBConstruct 1–153; UniProt 1–153 Author chain L; 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 1uxm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1uxm
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1uxm
Deposition date deposition_date2004-02-26
Structure title titleA4V mutant of human SOD1
Keywords keywordsHUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT, METAL- BINDING, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier50.32
Radius of gyration Rg (electron density) rg_electron50.38
Forward intensity I(0) i0617338000.00
Molecular weight molecular_weight191470.0 kDa
Excluded volume excluded_volume233770 ų
Envelope volume envelope_volume347190 ų
Hydration-shell volume shell_volume60238 ų
Envelope diameter envelope_diameter168.0
Shell Rg shell_rg50.05
Envelope Rg envelope_rg49.69
Shape Rg shape_rg50.39
Total Rg total_rg50.33
Total atoms total_atoms13368
Residues n_residues1836
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 dmax164.1
Rg (real space) rg_real50.45
Rg uncertainty (real space) rg_real_error1.78
I(0) (real space) i0_real6.1730e+08
I(0) uncertainty (real space) i0_real_error1.0940e+07
Rg (reciprocal space) rg_reciprocal50.20
I(0) (reciprocal space) i0_reciprocal617100000.0000
Solution quality estimate total_estimate0.8403
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.9
Skewness Skewness skewness0.331
Kurtosis Kurtosis kurtosis-0.519
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20440000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.944; Smooth: 0.173

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

Domain ID domain_idd1uxma_
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_idd1uxmb_
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_idd1uxmc_
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_idd1uxmd_
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_idd1uxme_
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_idd1uxmf_
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_idd1uxmg_
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_idd1uxmh_
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_idd1uxmi_
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_idd1uxmj_
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_idd1uxmk_
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_idd1uxml_
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 (12 domains)

Domain ID domain_id1uxmA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id1uxmB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id1uxmC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id1uxmD00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id1uxmE00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id1uxmF00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id1uxmG00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id1uxmH00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id1uxmI00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id1uxmJ00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id1uxmK00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id1uxmL00
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)