1sez

Crystal Structure of Protoporphyrinogen IX Oxidase

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

Protoporphyrinogen oxidase, mitochondrial

Nicotiana tabacum

UniProt O24164

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 FLAVIN-ADENINE DINUCLEOTIDE × 2 4-BROMO-3-(5'-CARBOXY-4'-CHLORO-2'-FLUOROPHENYL)-1-METHYL-5-TRIFLUOROMETHYL-PYRAZOL × 2 2-{2-[4-(1,1,3,3-TETRAMETHYLBUTYL)PHENOXY]ETHOXY}ETHANOL × 2 water × 2 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 4 FLAVIN-ADENINE DINUCLEOTIDE × 4 4-BROMO-3-(5'-CARBOXY-4'-CHLORO-2'-FLUOROPHENYL)-1-METHYL-5-TRIFLUOROMETHYL-PYRAZOL × 4 2-{2-[4-(1,1,3,3-TETRAMETHYLBUTYL)PHENOXY]ETHOXY}ETHANOL × 4 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PPOM_TOBAC
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–504; UniProt 1–504 Author chain B; PDBConstruct 1–504; UniProt 1–504

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_id1sez
Deposition date deposition_date2004-02-19
Structure title titleCrystal Structure of Protoporphyrinogen IX Oxidase
Keywords keywordsFAD-binding, Para-hydroxy-benzoate-hydroxylase fold (PHBH-fold), monotopic membrane-binding domain, 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.

1sez__assembly_1__model_1

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

Download this curve (.dat)

1sez__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1sez__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)37.36 Å
Rg (electron density)36.83 Å
Total Rg37.16 Å
Atom count7152
Residues912
Excluded volume127440 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1sez__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1sez__assembly_2__model_1 tetrameric (4) 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 (5)

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1seza1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.2 — FAD-linked reductases, N-terminal domain
Domain ID domain_idd1seza2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamilyd.16.1 — FAD-linked reductases, C-terminal domain
Family Family familyd.16.1.5 — L-aminoacid/polyamine oxidase
Domain ID domain_idd1sezb1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.2 — FAD-linked reductases, N-terminal domain
Domain ID domain_idd1sezb2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamilyd.16.1 — FAD-linked reductases, C-terminal domain
Family Family familyd.16.1.5 — L-aminoacid/polyamine oxidase

CATH v4.4 (6 domains)

Domain ID domain_id1sezA01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1sezA02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology660 — Polyamine Oxidase; Chain A, domain 2
Homologous superfamily homologous superfamily20 — Protoporphyrinogen oxidase, mitochondrial; domain 2
Domain ID domain_id1sezA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology3110 — protoporphyrinogen ix oxidase, domain 3
Homologous superfamily homologous superfamily10 — protoporphyrinogen ix oxidase, domain 3
Domain ID domain_id1sezB01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1sezB02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology660 — Polyamine Oxidase; Chain A, domain 2
Homologous superfamily homologous superfamily20 — Protoporphyrinogen oxidase, mitochondrial; domain 2
Domain ID domain_id1sezB03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology3110 — protoporphyrinogen ix oxidase, domain 3
Homologous superfamily homologous superfamily10 — protoporphyrinogen ix oxidase, domain 3
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7. Citations (1)