1t0s

Structure of the Toluene/o-Xylene Monooxygenase Hydroxylase with 4-bromophenol bound

Method: X-RAY DIFFRACTION

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

toluene, o-xylene monooxygenase oxygenase subunit

Pseudomonas stutzeri

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	toluene, o-xylene monooxygenase oxygenase subunit × 2 （O87802） touB × 2 （O87799） FE (III) ION × 4 HYDROXIDE ION × 2 SULFANYLACETIC ACID × 2 4-BROMOPHENOL × 12 water × 6	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	toluene, o-xylene monooxygenase oxygenase subunit × 1 （O87802） touB × 1 （O87799） FE (III) ION × 2 HYDROXIDE ION × 1 SULFANYLACETIC ACID × 1 4-BROMOPHENOL × 6 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O87798_PSEST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–498； UniProt 1–498

toluene, o-xylene monooxygenase oxygenase subunit

Pseudomonas stutzeri

UniProt O87802

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	toluene, o-xylene monooxygenase oxygenase subunit × 2 （O87798） touB × 2 （O87799） FE (III) ION × 4 HYDROXIDE ION × 2 SULFANYLACETIC ACID × 2 4-BROMOPHENOL × 12 water × 6	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	toluene, o-xylene monooxygenase oxygenase subunit × 1 （O87798） touB × 1 （O87799） FE (III) ION × 2 HYDROXIDE ION × 1 SULFANYLACETIC ACID × 1 4-BROMOPHENOL × 6 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O87802_PSEST
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–330； UniProt 1–330

touB

Pseudomonas stutzeri

UniProt O87799

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	toluene, o-xylene monooxygenase oxygenase subunit × 2 （O87798） toluene, o-xylene monooxygenase oxygenase subunit × 2 （O87802） FE (III) ION × 4 HYDROXIDE ION × 2 SULFANYLACETIC ACID × 2 4-BROMOPHENOL × 12 water × 6	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	toluene, o-xylene monooxygenase oxygenase subunit × 1 （O87798） toluene, o-xylene monooxygenase oxygenase subunit × 1 （O87802） FE (III) ION × 2 HYDROXIDE ION × 1 SULFANYLACETIC ACID × 1 4-BROMOPHENOL × 6 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O87799_PSEST
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–86； UniProt 1–86

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_id	1t0s
Deposition date deposition_date	2004-04-12
Structure title title	Structure of the Toluene/o-Xylene Monooxygenase Hydroxylase with 4-bromophenol bound
Keywords keywords	diiron, 4-bromophenol, channel, 4-helix bundle, carboxylate bridge, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method method	X-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.

1t0s__assembly_1__model_1

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

Download this curve (.dat)

1t0s__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1t0s__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	41.09 Å
Rg (electron density)	40.86 Å
Total Rg	41.18 Å
Atom count	14800
Residues	1794
Excluded volume	261040 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1t0s__assembly_1__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1t0s__assembly_2__model_1`	trimeric （3）	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 (8)

Entity 1 Entity 1 polymer

Description description	toluene, o-xylene monooxygenase oxygenase subunit
Molecular weight formula_weight	57786.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	7667

MSMLKREDWYDLTRTTNWTPKYVTENELFPEEMSGARGISMEAWEKYDEPYKITYPEYVSIQREKDSGAYSIKAALERDGFVDRADPGWVSTMQLHFGAIALEEYAASTAEARMARFAKAPGNRNMATFGMMDENRHGQIQLYFPYANVKRSRKWDWAHKAIHTNEWAAIAARSFFDDMMMTRDSVAVSIMLTFAFETGFTNMQFLGLAADAAEAGDHTFASLISSIQTDESRHAQQGGPSLKILVENGKKDEAQQMVDVAIWRSWKLFSVLTGPIMDYYTPLESRNQSFKEFMLEWIVAQFERQLLDLGLDKPWYWDQFMQDLDETHHGMHLGVWYWRPTVWWDPAAGVSPEEREWLEEKYPGWNDTWGQCWDVITDNLVNGKPELTVPETLPTICNMCNLPIAHTPGNKWNVKDYQLEYEGRLYHFGSEADRWCFQIDPERYKNHTNLVDRFLKGEIQPADLAGALMYMSLEPGVMGDDAHDYEWVKAYQKKTNAA

Source Source

Source organism organism	Pseudomonas stutzeri
NCBI taxonomy ID ncbi_taxonomy_id	316
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	toluene, o-xylene monooxygenase oxygenase subunit
Molecular weight formula_weight	38381.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MSEQQPEALKPLKTWSHLAGNRRRPSEYEVVSTNLHYFTDNPERPWELDSNLPMQTWYKKYCFDSPLKHDDWNAFRDPDQLVYRTYNLLQDGQESYVQGLFDQLNDRGHDQMLTREWVETLARFYTPARYLFHALQMGSVYIHQIAPASTITNCATYETADHLRWLTHTAYRTRELANCYPDVGFGKRERDVWENDPAWQGFRELIEKALIAWDWGEAFTAINLVTKPAVEEALLQQLGSLAQSEGDTLLGLLAQAQKRDAERHRRWSSALVKMALEKEGNREVLQKWVAKWEPLADKAIEAYCSALPDGENAIVEAKSASRYVRQMMGL

Source Source

Source organism organism	Pseudomonas stutzeri
NCBI taxonomy ID ncbi_taxonomy_id	316
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 polymer

Description description	touB
Molecular weight formula_weight	9986.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

MATFPIMSNFERDFVIQLVPVDTEDTMDQVAEKCAYHSINRRVHPQPEKILRVRRHEDGTLFPRGMIVSDAGLRPTETLDIIFMDN

Source Source

Source organism organism	Pseudomonas stutzeri
NCBI taxonomy ID ncbi_taxonomy_id	316
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 4 Entity 4 non-polymer

Description description	FE (III) ION
Molecular weight formula_weight	55.8 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	HYDROXIDE ION
Molecular weight formula_weight	17.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	SULFANYLACETIC ACID
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 non-polymer

Description description	4-BROMOPHENOL
Molecular weight formula_weight	173.0 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 8 Entity 8 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	267

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1t0sa_
Class class	a — All alpha proteins
Fold Fold fold	a.25 — Ferritin-like
Superfamily Superfamily superfamily	a.25.1 — Ferritin-like
Family Family family	a.25.1.2 — Ribonucleotide reductase-like

Domain ID domain_id	d1t0sb_
Class class	a — All alpha proteins
Fold Fold fold	a.25 — Ferritin-like
Superfamily Superfamily superfamily	a.25.1 — Ferritin-like
Family Family family	a.25.1.2 — Ribonucleotide reductase-like

Domain ID domain_id	d1t0sc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.12 — TmoB-like
Family Family family	d.15.12.1 — TmoB-like

CATH v4.4 (3 domains)

Domain ID domain_id	1t0sA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	620 — Ribonucleotide Reductase, subunit A
Homologous superfamily homologous superfamily	20 — Ribonucleotide Reductase, subunit A

Domain ID domain_id	1t0sB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	620 — Ribonucleotide Reductase, subunit A
Homologous superfamily homologous superfamily	20 — Ribonucleotide Reductase, subunit A

Domain ID domain_id	1t0sC00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	270 — TmoB-like

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Unit-cell length a length_a	183.242 Å
Unit-cell length b length_b	183.242 Å
Unit-cell length c length_c	67.671 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	29.470 Å
R factor r_factor	0.2360
R_work r_work	0.2360
R_free r_free	0.2730

Structure of the Toluene/o-Xylene Monooxygenase Hydroxylase with 4-bromophenol bound

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

toluene, o-xylene monooxygenase oxygenase subunit

State in the Current Structure

Other States of the Same Protein in the Database

toluene, o-xylene monooxygenase oxygenase subunit

State in the Current Structure

Other States of the Same Protein in the Database

touB

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1t0s__assembly_1__model_1

1t0s__assembly_1__model_1 | I(q)

1t0s__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)

Structure of the Toluene/o-Xylene Monooxygenase Hydroxylase with 4-bromophenol bound

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

toluene, o-xylene monooxygenase oxygenase subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

toluene, o-xylene monooxygenase oxygenase subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

touB

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1t0s__assembly_1__model_1

1t0s__assembly_1__model_1 | I(q)

1t0s__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)