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1olt

Coproporphyrinogen III oxidase (HemN) from Escherichia coli is a Radical SAM enzyme.

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

OXYGEN-INDEPENDENT COPROPORPHYRINOGEN III OXIDASE

OrganismNot specified

UniProt P32131

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 IRON/SULFUR CLUSTER × 1 S-ADENOSYLMETHIONINE × 2 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1olt

1 assemblies

Homodimer

None

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex

None

View Construct and Data Evidence
UniProt name HEMN_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–457； UniProt 1–457

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_id1olt
Deposition date deposition_date2003-08-13
Structure title titleCoproporphyrinogen III oxidase (HemN) from Escherichia coli is a Radical SAM enzyme.
Keywords keywordsHEME BIOSYNTHESIS, DECARBOXYLASE, RADICAL SAM ENZYME, 4FE- 4S CLUSTER, S-ADENOSYL-L-METHIONINE, OXIDOREDUCTASE; OXIDOREDUCTASE
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.

1olt__assembly_1__model_1

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

Download this curve (.dat)

1olt__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.

1olt__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）22.71 Å
Rg (electron density)21.77 Å
Total Rg22.54 Å
Atom count3586
Residues434
Excluded volume63670 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1olt__assembly_1__model_1 monomeric （1） 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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1olta_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.28 — Radical SAM enzymes
Family Family familyc.1.28.2 — Oxygen-independent coproporphyrinogen III oxidase HemN

CATH v4.4 (1 domains)

Domain ID domain_id1oltA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily920 —
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7. Citations (1)