1isc

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

Method: X-RAY DIFFRACTION
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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 AZIDE 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id1isc
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
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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.

1isc__assembly_1__model_1

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

Download this curve (.dat)

1isc__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.

1isc__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)22.79 Å
Rg (electron density)22.00 Å
Total Rg23.00 Å
Atom count3014
Residues384
Excluded volume53165 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1isc__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1isca1
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_idd1isca2
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_idd1iscb1
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_idd1iscb2
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
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7. Citations (3)