4bd4

Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, mutant H43F

Method: X-RAY DIFFRACTION Dmax: 114.2 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–49 Chain A; UniProt 83–124 Chain A; UniProt 141–154 Mutation:YES GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:18 % PEG 1500, 15% GLYCEROL Resolution 2.78 Å R-free 0.246
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–49 Chain B; UniProt 83–124 Chain B; UniProt 141–154 Mutation:YES GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:18 % PEG 1500, 15% GLYCEROL Resolution 2.78 Å R-free 0.246
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 2–49 Chain C; UniProt 83–124 Chain C; UniProt 141–154 Mutation:YES No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:18 % PEG 1500, 15% GLYCEROL Resolution 2.78 Å R-free 0.246
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 2–49 Chain D; UniProt 83–124 Chain D; UniProt 141–154 Mutation:YES No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:18 % PEG 1500, 15% GLYCEROL Resolution 2.78 Å R-free 0.246
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 2–49 Chain E; UniProt 83–124 Chain E; UniProt 141–154 Mutation:YES No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:18 % PEG 1500, 15% GLYCEROL Resolution 2.78 Å R-free 0.246
6 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 2–49 Chain F; UniProt 83–124 Chain F; UniProt 141–154 Mutation:YES No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:18 % PEG 1500, 15% GLYCEROL Resolution 2.78 Å R-free 0.246
7 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain G; UniProt 2–49 Chain G; UniProt 83–124 Chain G; UniProt 141–154 Mutation:YES GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:18 % PEG 1500, 15% GLYCEROL Resolution 2.78 Å R-free 0.246
8 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain H; UniProt 2–49 Chain H; UniProt 83–124 Chain H; UniProt 141–154 Mutation:YES GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:18 % PEG 1500, 15% GLYCEROL Resolution 2.78 Å R-free 0.246
9 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain I; UniProt 2–49 Chain I; UniProt 83–124 Chain I; UniProt 141–154 Mutation:YES No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:18 % PEG 1500, 15% GLYCEROL Resolution 2.78 Å R-free 0.246

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 367 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 1–48; UniProt 2–49 Author chain A; PDBConstruct 52–93; UniProt 83–124 Author chain A; PDBConstruct 97–110; UniProt 141–154 Author chain B; PDBConstruct 1–48; UniProt 2–49 Author chain B; PDBConstruct 52–93; UniProt 83–124 Author chain B; PDBConstruct 97–110; UniProt 141–154 Author chain C; PDBConstruct 1–48; UniProt 2–49 Author chain C; PDBConstruct 52–93; UniProt 83–124 Author chain C; PDBConstruct 97–110; UniProt 141–154 Author chain D; PDBConstruct 1–48; UniProt 2–49 Author chain D; PDBConstruct 52–93; UniProt 83–124 Author chain D; PDBConstruct 97–110; UniProt 141–154 Author chain E; PDBConstruct 1–48; UniProt 2–49 Author chain E; PDBConstruct 52–93; UniProt 83–124 Author chain E; PDBConstruct 97–110; UniProt 141–154 Author chain F; PDBConstruct 1–48; UniProt 2–49 Author chain F; PDBConstruct 52–93; UniProt 83–124 Author chain F; PDBConstruct 97–110; UniProt 141–154 Author chain G; PDBConstruct 1–48; UniProt 2–49 Author chain G; PDBConstruct 52–93; UniProt 83–124 Author chain G; PDBConstruct 97–110; UniProt 141–154 Author chain H; PDBConstruct 1–48; UniProt 2–49 Author chain H; PDBConstruct 52–93; UniProt 83–124 Author chain H; PDBConstruct 97–110; UniProt 141–154 Author chain I; PDBConstruct 1–48; UniProt 2–49 Author chain I; PDBConstruct 52–93; UniProt 83–124 Author chain I; PDBConstruct 97–110; UniProt 141–154

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 4bd4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4bd4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4bd4
Deposition date deposition_date2012-10-04
Structure title titleMonomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, mutant H43F
Keywords keywordsOXIDOREDUCTASE, CU/ZN SOD1, MONOMERIC MUTANT, DISEASE MUTATION, METAL BINDING, NEURODEGENERATION, ALS; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.40
Radius of gyration Rg (electron density) rg_electron34.80
Forward intensity I(0) i0142737000.00
Molecular weight molecular_weight95128.0 kDa
Excluded volume excluded_volume119230 ų
Envelope volume envelope_volume167740 ų
Hydration-shell volume shell_volume40954 ų
Envelope diameter envelope_diameter118.7
Shell Rg shell_rg40.54
Envelope Rg envelope_rg34.13
Shape Rg shape_rg34.79
Total Rg total_rg35.28
Total atoms total_atoms6742
Residues n_residues940
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 dmax114.2
Rg (real space) rg_real35.37
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real1.4270e+08
I(0) uncertainty (real space) i0_real_error2.3160e+06
Rg (reciprocal space) rg_reciprocal35.39
I(0) (reciprocal space) i0_reciprocal142700000.0000
Solution quality estimate total_estimate0.8904
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.7
Skewness Skewness skewness0.245
Kurtosis Kurtosis kurtosis-0.445
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18780000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.934; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.773

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 9 domains

CATH v4.4 (9 domains)

Domain ID domain_id4bd4A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id4bd4B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id4bd4C00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id4bd4D00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id4bd4E00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id4bd4F00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id4bd4G00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id4bd4H00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id4bd4I00
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)