SAXSdb — 3fmw

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

Oxygenase

Streptomyces argillaceus

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 1,2-ETHANEDIOL × 1 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	FLAVIN-ADENINE DINUCLEOTIDE × 2 1,2-ETHANEDIOL × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q194P4_STRAA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 38–570； UniProt 1–533 Author chain B； PDBConstruct 38–570； UniProt 1–533 Author chain C； PDBConstruct 38–570； UniProt 1–533

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	3fmw
Deposition date deposition_date	2008-12-22
Structure title title	The crystal structure of MtmOIV, a Baeyer-Villiger monooxygenase from the mithramycin biosynthetic pathway in Streptomyces argillaceus.
Keywords keywords	oxygenase, mithramycin, Baeyer-Villiger, flavin binding protein, 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.

3fmw__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3fmw__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3fmw__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	34.62 Å
Rg (electron density)	34.36 Å
Total Rg	34.80 Å
Atom count	6818
Residues	958
Excluded volume	119530 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3fmw__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3fmw__assembly_2__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)

Entity 1 Entity 1 polymer

Description description	Oxygenase
Molecular weight formula_weight	61263.9 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	10370

MRGSHHHHHHGMASMTGGNNMGRDLYDDDDKDPGRRMMHNSNADDAALTTDVVVVGGGPVGLMLAGELRAGGVGALVLEKLVEPVGHDRAGALHIRTVETLDLRGLLDRFLEGTQVAKGLPFAGIFTQGLDFGLVDTRHPYTGLVPQSRTEALLAEHAREAGAEIPRGHEVTRLRQDAEAVEVTVAGPSGPYPVRARYGVGCDGGRSTVRRLAADRFPGTEATVRALIGYVTTPEREVPRRWERTPDGILVLAFPPEGGLGPGWSSSSTGHSPAADEGPVTLEDLGAAVARVRGTPLTLTEPVSWLSRFGDASRQAKRYRSGRVLLAGDAAHVHFPIGGQGLNTGLQDAVNLGWKLAARVRGWGSEELLDTYHDERHPVAERVLLNTRAQLALMRPDEQHTTPLRGFVEELLGTDEVNRYFTGMITGTDVRYATFAPAASARPHPWPGRFAGGLVLSRPSGEPVPVAELLRSARPLLLDLAGRADLREATRPWSDRVSVVAGEATVEPPAQALLVRPDGYVAWAGSPAATADELRASLARWFGPPANREPVGHQERAGRRGRPLSALKPE

Source Source

Source organism organism	Streptomyces argillaceus
NCBI taxonomy ID ncbi_taxonomy_id	41951
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 3 Entity 3 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	18

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6. Fold Classification (SCOP + CATH) 9 domains

CATH v4.4 (9 domains)

Domain ID domain_id	3fmwA01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	3fmwA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	2450 —

Domain ID domain_id	3fmwA03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	120 —

Domain ID domain_id	3fmwB01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	3fmwB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	2450 —

Domain ID domain_id	3fmwB03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	120 —

Domain ID domain_id	3fmwC01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	3fmwC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	2450 —

Domain ID domain_id	3fmwC03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	120 —

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Unit-cell length a length_a	145.265 Å
Unit-cell length b length_b	114.437 Å
Unit-cell length c length_c	138.563 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.03 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.890 Å
Low-resolution limit resolution_low	29.680 Å
R factor r_factor	0.2370
R_work r_work	0.2350
R_free r_free	0.2730

The crystal structure of MtmOIV, a Baeyer-Villiger monooxygenase from the mithramycin biosynthetic pathway in Streptomyces argillaceus.

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

Oxygenase

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

3fmw__assembly_2__model_1

3fmw__assembly_2__model_1 | I(q)

3fmw__assembly_2__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 9 domains

CATH v4.4 (9 domains)

7. Citations (1)

The crystal structure of MtmOIV, a Baeyer-Villiger monooxygenase from the mithramycin biosynthetic pathway in Streptomyces argillaceus.

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

Oxygenase

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

3fmw__assembly_2__model_1

3fmw__assembly_2__model_1 | I(q)

3fmw__assembly_2__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 9 domains

CATH v4.4 (9 domains)

7. Citations (1)