4p1b

CRYSTAL STRUCTURE OF THE TOLUENE 4-MONOOXYGENASE HYDROXYLASE-FERREDOXIN C7S E16C C84A C85A VARIANT ELECTRON-TRANSFER COMPLEX

Method: X-RAY DIFFRACTION

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

Toluene-4-monooxygenase system protein A

Pseudomonas mendocina

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 8	Toluene-4-monooxygenase system protein E × 2 （Q00460） Toluene-4-monooxygenase system protein B × 2 （Q00457） Toluene-4-monooxygenase system ferredoxin subunit × 2 （Q00458） FE (III) ION × 4 ACETATE ION × 7 SODIUM ION × 1 DI(HYDROXYETHYL)ETHER × 1 FE2/S2 (INORGANIC) CLUSTER × 2 water × 8	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TMOA_PSEME
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–490； UniProt 2–491 Author chain D； PDBConstruct 1–490； UniProt 2–491

Toluene-4-monooxygenase system protein E

Pseudomonas mendocina

UniProt Q00460

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 8	Toluene-4-monooxygenase system protein A × 2 （Q00456） Toluene-4-monooxygenase system protein B × 2 （Q00457） Toluene-4-monooxygenase system ferredoxin subunit × 2 （Q00458） FE (III) ION × 4 ACETATE ION × 7 SODIUM ION × 1 DI(HYDROXYETHYL)ETHER × 1 FE2/S2 (INORGANIC) CLUSTER × 2 water × 8	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TMOE_PSEME
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–305； UniProt 2–306 Author chain E； PDBConstruct 1–305； UniProt 2–306

Toluene-4-monooxygenase system protein B

Pseudomonas mendocina

UniProt Q00457

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 8	Toluene-4-monooxygenase system protein A × 2 （Q00456） Toluene-4-monooxygenase system protein E × 2 （Q00460） Toluene-4-monooxygenase system ferredoxin subunit × 2 （Q00458） FE (III) ION × 4 ACETATE ION × 7 SODIUM ION × 1 DI(HYDROXYETHYL)ETHER × 1 FE2/S2 (INORGANIC) CLUSTER × 2 water × 8	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TMOB_PSEME
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–82； UniProt 2–83 Author chain F； PDBConstruct 1–82； UniProt 2–83

Toluene-4-monooxygenase system ferredoxin subunit

Pseudomonas mendocina

UniProt Q00458

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 8	Toluene-4-monooxygenase system protein A × 2 （Q00456） Toluene-4-monooxygenase system protein E × 2 （Q00460） Toluene-4-monooxygenase system protein B × 2 （Q00457） FE (III) ION × 4 ACETATE ION × 7 SODIUM ION × 1 DI(HYDROXYETHYL)ETHER × 1 FE2/S2 (INORGANIC) CLUSTER × 2 water × 8	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TMOC_PSEME
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain H； PDBConstruct 1–111； UniProt 2–112 Author chain I； PDBConstruct 1–111； UniProt 2–112

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	4p1b
Deposition date deposition_date	2014-02-25
Structure title title	CRYSTAL STRUCTURE OF THE TOLUENE 4-MONOOXYGENASE HYDROXYLASE-FERREDOXIN C7S E16C C84A C85A VARIANT ELECTRON-TRANSFER COMPLEX
Keywords keywords	ELECTRON-TRANSFER COMPLEX, OXIDOREDUCTASE, DIIRON ENZYME COMPLEX, IRON-SULFUR, REDUCTION, HYDROXYLASE FERREDOXIN, OXYGENASE; 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.

4p1b__assembly_1__model_1

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

Download this curve (.dat)

4p1b__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4p1b__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	40.24 Å
Rg (electron density)	39.82 Å
Total Rg	40.19 Å
Atom count	16186
Residues	1976
Excluded volume	284890 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4p1b__assembly_1__model_1`	octameric （8）	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 (10)

Entity 1 Entity 1 polymer

Description description	Toluene-4-monooxygenase system protein A
Molecular weight formula_weight	57089.9 kDa
EC 编号 ec_number	1.14.13.-
Mutation mutation	Stop 492
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D
Atom count atom_count	18244

AMHPRKDWYELTRATNWTPSYVTEEQLFPERMSGHMGIPLEKWESYDEPYKTSYPEYVSIQREKDAGAYSVKAALERAKIYENSDPGWISTLKSHYGAIAVGEYAAVTGEGRMARFSKAPGNRNMATFGMMDELRHGQLQLFFPHEYCKKDRQFDWAWRAYHSNEWAAIAAKHFFDDIITGRDAISVAIMLTFSFETGFTNMQFLGLAADAAEAGDYTFANLISSIQTDESRHAQQGGPALQLLIENGKREEAQKKVDMAIWRAWRLFAVLTGPVMDYYTPLEDRSQSFKEFMYEWIIGQFERSLIDLGLDKPWYWDLFLKDIDELHHSYHMGVWYWRTTAWWNPAAGVTPEERDWLEEKYPGWNKRWGRCWDVITENVLNDRMDLVSPETLPSVCNMSQIPLVGVPGDDWNIEVFSLEHNGRLYHFGSEVDRWVFQQDPVQYQNHMNIVDRFLAGQIQPMTLEGALKYMGFQSIEEMGKDAHDFAWADK

Source Source

Source organism organism	Pseudomonas mendocina
NCBI taxonomy ID ncbi_taxonomy_id	300
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Toluene-4-monooxygenase system protein E
Molecular weight formula_weight	35930.4 kDa
EC 编号 ec_number	1.14.13.-
Mutation mutation	Stop 307
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,E

SFESKKPMRTWSHLAEMRKKPSEYDIVSRKLHYSTNNPDSPWELSPDSPMNLWYKQYRNASPLKHDNWDAFTDPDQLVYRTYNLMQDGQESYVQSLFDQFNEREHDQMVREGWEHTMARCYSPLRYLFHCLQMSSAYVQQMAPASTISNCCILQTADSLRWLTHTAYRTHELSLTYPDAGLGEHERELWEKEPGWQGLRELMEKQLTAFDWGEAFVSLNLVVKPMIVESIFKPLQQQAWENNDTLLPLLIDSQLKDAERHSRWSKALVKHALENPDNHAVIEGWIEKWRPLADRAAEAYLSMLSS

Source Source

Source organism organism	Pseudomonas mendocina
NCBI taxonomy ID ncbi_taxonomy_id	300
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Toluene-4-monooxygenase system protein B
Molecular weight formula_weight	9340.7 kDa
EC 编号 ec_number	1.14.13.-
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,F

SAFPVHAAFEKDFLVQLVVVDLNDSMDQVAEKVAYHCVNRRVAPREGVMRVRKHRSTELFPRDMTIAESGLNPTEVIDVVFE

Source Source

Source organism organism	Pseudomonas mendocina
NCBI taxonomy ID ncbi_taxonomy_id	300
Host organism host_organism	Escherichia coli

Entity 4 Entity 4 polymer

Description description	Toluene-4-monooxygenase system ferredoxin subunit
Molecular weight formula_weight	12099.3 kDa
Mutation mutation	C7S, E16C, C84A,C85A
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,I

SFEKISSLDDIWVGCMETFETSDGTEVLIVNSEEHGVKAYQAMCPHQEILLSEGSYEGGVITCRAHLWTFNDGTGHGINPDDAALAEYPVEVKGDDIYVSTKGILPNKAHS

Source Source

Source organism organism	Pseudomonas mendocina
NCBI taxonomy ID ncbi_taxonomy_id	300
Host organism host_organism	Escherichia coli

Entity 5 Entity 5 non-polymer

Description description	FE (III) ION
Molecular weight formula_weight	55.8 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 6 Entity 6 non-polymer

Description description	ACETATE ION
Molecular weight formula_weight	59.0 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 7 Entity 7 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 8 Entity 8 non-polymer

Description description	DI(HYDROXYETHYL)ETHER
Molecular weight formula_weight	106.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 9 Entity 9 non-polymer

Description description	FE2/S2 (INORGANIC) CLUSTER
Molecular weight formula_weight	175.8 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 10 Entity 10 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1917

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6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d4p1ba_
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	d4p1bc_
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.15.12.0 — automated matches

Domain ID domain_id	d4p1bd_
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	d4p1bf_
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.15.12.0 — automated matches

Domain ID domain_id	d4p1bh_
Class class	b — All beta proteins
Fold Fold fold	b.33 — ISP domain
Superfamily Superfamily superfamily	b.33.1 — ISP domain
Family Family family	b.33.1.1 — Rieske iron-sulfur protein (ISP)

Domain ID domain_id	d4p1bi_
Class class	b — All beta proteins
Fold Fold fold	b.33 — ISP domain
Superfamily Superfamily superfamily	b.33.1 — ISP domain
Family Family family	b.33.1.1 — Rieske iron-sulfur protein (ISP)

CATH v4.4 (8 domains)

Domain ID domain_id	4p1bA00
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	4p1bB00
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	4p1bC00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	270 — TmoB-like

Domain ID domain_id	4p1bD00
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	4p1bE00
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	4p1bF00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	270 — TmoB-like

Domain ID domain_id	4p1bH00
Class class	2 — Mainly Beta
Architecture architecture	102 — 3-layer Sandwich
Topology topology	10 — Rieske Iron-sulfur Protein
Homologous superfamily homologous superfamily	10 — Rieske [2Fe-2S] iron-sulphur domain

Domain ID domain_id	4p1bI00
Class class	2 — Mainly Beta
Architecture architecture	102 — 3-layer Sandwich
Topology topology	10 — Rieske Iron-sulfur Protein
Homologous superfamily homologous superfamily	10 — Rieske [2Fe-2S] iron-sulphur domain

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Unit-cell length a length_a	128.367 Å
Unit-cell length b length_b	128.367 Å
Unit-cell length c length_c	284.460 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	12

Space group space_group	P 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	2.050 Å
Low-resolution limit resolution_low	47.950 Å
R factor r_factor	0.1480
R_work r_work	0.1460
R_free r_free	0.1770

CRYSTAL STRUCTURE OF THE TOLUENE 4-MONOOXYGENASE HYDROXYLASE-FERREDOXIN C7S E16C C84A C85A VARIANT ELECTRON-TRANSFER COMPLEX

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

Toluene-4-monooxygenase system protein A

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-4-monooxygenase system protein E

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-4-monooxygenase system protein B

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-4-monooxygenase system ferredoxin 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

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4p1b__assembly_1__model_1

4p1b__assembly_1__model_1 | I(q)

4p1b__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 (10)

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 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 water

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (6 domains)

CATH v4.4 (8 domains)

7. Citations (1)