1mfm

MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 49.0 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (COPPER,ZINC SUPEROXIDE DISMUTASE)

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 1–153 Mutation:C6A,F50E,G51E,C111S,E133Q ZN ZINC ION × 1 CU COPPER (II) ION × 1 CD CADMIUM ION × 9 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;PEG 6000 15%, CDCL2 200-400 MM, TRIS 100MM, PH=8, pH 8.0 Resolution 1.02 Å

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 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 1mfm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1mfm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1mfm
Deposition date deposition_date1999-04-16
Structure title titleMONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION
Keywords keywordsOXIDOREDUCTASE, SUPEROXIDE ACCEPTOR, MONOMERIC MUTANT; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.79
Radius of gyration Rg (electron density) rg_electron14.46
Forward intensity I(0) i07216610.00
Molecular weight molecular_weight16808.0 kDa
Excluded volume excluded_volume19591 ų
Envelope volume envelope_volume22260 ų
Hydration-shell volume shell_volume13067 ų
Envelope diameter envelope_diameter48.5
Shell Rg shell_rg20.22
Envelope Rg envelope_rg14.71
Shape Rg shape_rg14.26
Total Rg total_rg15.86
Total atoms total_atoms1111
Residues n_residues153
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 dmax49.0
Rg (real space) rg_real15.68
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real7.2170e+06
I(0) uncertainty (real space) i0_real_error8.4240e+04
Rg (reciprocal space) rg_reciprocal15.69
I(0) (reciprocal space) i0_reciprocal7217000.0000
Solution quality estimate total_estimate0.9012
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.5
Skewness Skewness skewness0.100
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha570200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1mfma_
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 (1 domains)

Domain ID domain_id1mfmA00
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)