5u9m

Copper-Zinc Superoxide Dismutase is Activated through a Sulfenic Acid Intermediate at a Copper-ion Entry Site

Method: X-RAY DIFFRACTION Dmax: 116.0 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–154 Mutation:H46R,H48Q Superoxide dismutase 1 copper chaperone × 1 (P40202) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;25 % PEG 3350, 0.2 M ammonium sulfate, 0.1 M bis-tris pH 6.5 Resolution 2.35 Å R-free 0.235
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 2–154 Mutation:H46R,H48Q Superoxide dismutase 1 copper chaperone × 1 (P40202) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;25 % PEG 3350, 0.2 M ammonium sulfate, 0.1 M bis-tris pH 6.5 Resolution 2.35 Å R-free 0.235

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 C; PDBConstruct 1–153; UniProt 2–154

Superoxide dismutase 1 copper chaperone

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P40202

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2–249 Mutation:E238A,E239A,R240A Superoxide dismutase [Cu-Zn] × 1 (P00441) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;25 % PEG 3350, 0.2 M ammonium sulfate, 0.1 M bis-tris pH 6.5 Resolution 2.35 Å R-free 0.235
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2–249 Mutation:E238A,E239A,R240A Superoxide dismutase [Cu-Zn] × 1 (P00441) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;25 % PEG 3350, 0.2 M ammonium sulfate, 0.1 M bis-tris pH 6.5 Resolution 2.35 Å R-free 0.235

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.

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCS1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–248; UniProt 2–249 Author chain D; PDBConstruct 1–248; UniProt 2–249

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 5u9m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5u9m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5u9m
Deposition date deposition_date2016-12-16
Structure title titleCopper-Zinc Superoxide Dismutase is Activated through a Sulfenic Acid Intermediate at a Copper-ion Entry Site
Keywords keywordsoxidoreductase-chaperone complex, Cu-Zn superoxide dismutase, metallochaperone; oxidoreductase/chaperone
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.20
Radius of gyration Rg (electron density) rg_electron31.61
Forward intensity I(0) i0113052000.00
Molecular weight molecular_weight81775.0 kDa
Excluded volume excluded_volume101340 ų
Envelope volume envelope_volume131600 ų
Hydration-shell volume shell_volume35958 ų
Envelope diameter envelope_diameter122.1
Shell Rg shell_rg36.98
Envelope Rg envelope_rg31.58
Shape Rg shape_rg31.54
Total Rg total_rg32.27
Total atoms total_atoms5737
Residues n_residues766
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 dmax116.0
Rg (real space) rg_real32.37
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real1.1310e+08
I(0) uncertainty (real space) i0_real_error2.1110e+06
Rg (reciprocal space) rg_reciprocal32.30
I(0) (reciprocal space) i0_reciprocal113000000.0000
Solution quality estimate total_estimate0.8497
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.9
Skewness Skewness skewness0.490
Kurtosis Kurtosis kurtosis-0.109
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19080000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.731; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.888; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd5u9ma_
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_idd5u9mb1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.17 — HMA, heavy metal-associated domain
Family Family familyd.58.17.0 — automated matches
Domain ID domain_idd5u9mb2
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_idd5u9mc_
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_idd5u9md1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.17 — HMA, heavy metal-associated domain
Family Family familyd.58.17.0 — automated matches
Domain ID domain_idd5u9md2
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

8. Citations (1)

9. Files and Curves (10)