1isb

STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS

Method: X-RAY DIFFRACTION

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

IRON(III) SUPEROXIDE DISMUTASE

Escherichia coli

UniProt P09157

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 FE (III) ION × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name SODF_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–192; UniProt 1–192 Author chain B; PDBConstruct 1–192; UniProt 1–192

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.

2. Structure Basics 2. Structure Basics

Entry ID entry_id1isb
Deposition date deposition_date1994-07-12
Structure title titleSTRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS
Keywords keywordsOXIDOREDUCTASE(SUPEROXIDE ACCEPTOR); OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR)
Experimental Method methodX-RAY DIFFRACTION

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1isb__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1isb__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1isb__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)22.83 Å
Rg (electron density)22.01 Å
Total Rg23.01 Å
Atom count3008
Residues384
Excluded volume53150 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1isb__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (3)

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1isba1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.11 — Fe,Mn superoxide dismutase (SOD), N-terminal domain
Family Family familya.2.11.1 — Fe,Mn superoxide dismutase (SOD), N-terminal domain
Domain ID domain_idd1isba2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.44 — Fe,Mn superoxide dismutase (SOD), C-terminal domain
Superfamily Superfamily superfamilyd.44.1 — Fe,Mn superoxide dismutase (SOD), C-terminal domain
Family Family familyd.44.1.1 — Fe,Mn superoxide dismutase (SOD), C-terminal domain
Domain ID domain_idd1isbb1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.11 — Fe,Mn superoxide dismutase (SOD), N-terminal domain
Family Family familya.2.11.1 — Fe,Mn superoxide dismutase (SOD), N-terminal domain
Domain ID domain_idd1isbb2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.44 — Fe,Mn superoxide dismutase (SOD), C-terminal domain
Superfamily Superfamily superfamilyd.44.1 — Fe,Mn superoxide dismutase (SOD), C-terminal domain
Family Family familyd.44.1.1 — Fe,Mn superoxide dismutase (SOD), C-terminal domain

7. Citations (3)