1o95

Ternary complex between trimethylamine dehydrogenase and electron transferring flavoprotein

Method: X-RAY DIFFRACTION

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

TRIMETHYLAMINE DEHYDROGENASE

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT × 2 （P53570） ELECTRON TRANSFER FLAVOPROTEIN ALPHA-SUBUNIT × 2 （P53571） FLAVIN MONONUCLEOTIDE × 2 ADENOSINE-5'-DIPHOSPHATE × 2 IRON/SULFUR CLUSTER × 2 ADENOSINE MONOPHOSPHATE × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DHTM_METME
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–729； UniProt 1–729 Author chain B； PDBConstruct 1–729； UniProt 1–729

ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT

METHYLOPHILUS METHYLOTROPHUS

UniProt P53570

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	TRIMETHYLAMINE DEHYDROGENASE × 2 （P16099） ELECTRON TRANSFER FLAVOPROTEIN ALPHA-SUBUNIT × 2 （P53571） FLAVIN MONONUCLEOTIDE × 2 ADENOSINE-5'-DIPHOSPHATE × 2 IRON/SULFUR CLUSTER × 2 ADENOSINE MONOPHOSPHATE × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ETFB_METME
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–264； UniProt 1–264 Author chain E； PDBConstruct 1–264； UniProt 1–264

ELECTRON TRANSFER FLAVOPROTEIN ALPHA-SUBUNIT

METHYLOPHILUS METHYLOTROPHUS

UniProt P53571

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	TRIMETHYLAMINE DEHYDROGENASE × 2 （P16099） ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT × 2 （P53570） FLAVIN MONONUCLEOTIDE × 2 ADENOSINE-5'-DIPHOSPHATE × 2 IRON/SULFUR CLUSTER × 2 ADENOSINE MONOPHOSPHATE × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ETFA_METME
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain D； PDBConstruct 1–320； UniProt 1–320 Author chain F； PDBConstruct 1–320； UniProt 1–320

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	1o95
Deposition date deposition_date	2002-12-11
Structure title title	Ternary complex between trimethylamine dehydrogenase and electron transferring flavoprotein
Keywords keywords	;ELECTRON TRANSPORT-COMPLEX, PROTEIN COMPLEX, ELECTRON TRANSFER, DEHYDROGENASE, ELECTRON TRANSPORT, FLAVOPROTEIN, OXIDO-REDUCTASE, IRON-SULFUR, FMN ;; ELECTRON TRANSPORT
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.

1o95__assembly_1__model_1

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

Download this curve (.dat)

1o95__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1o95__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	48.55 Å
Rg (electron density)	49.98 Å
Total Rg	49.86 Å
Atom count	17776
Residues	2305
Excluded volume	313760 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1o95__assembly_1__model_1`	hexameric （6）	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 (7)

Entity 1 Entity 1 polymer

Description description	TRIMETHYLAMINE DEHYDROGENASE
Molecular weight formula_weight	81606.0 kDa
EC 编号 ec_number	1.5.99.7
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	17776

ARDPKHDILFEPIQIGPKTLRNRFYQVPHCIGAGSDKPGFQSAHRSVKAEGGWAALNTEYCSINPESDDTHRLSARIWDEGDVRNLKAMTDEVHKYGALAGVELWYGGAHAPNMESRATPRGPSQYASEFETLSYCKEMDLSDIAQVQQFYVDAAKRSRDAGFDIVYVYGAHSYLPLQFLNPYYNKRTDKYGGSLENRARFWLETLEKVKHAVGSDCAIATRFGVDTVYGPGQIEAEVDGQKFVEMADSLVDMWDITIGDIAEWGEDAGPSRFYQQGHTIPWVKLVKQVSKKPVLGVGRYTDPEKMIEIVTKGYADIIGCARPSIADPFLPQKVEQGRYDDIRVCIGCNVCISRWEIGGPPMICTQNATAGEEYRRGWHPEKFRQTKNKDSVLIVGAGPSGSEAARVLMESGYTVHLTDTAEKIGGHLNQVAALPGLGEWSYHRDYRETQITKLLKKNKESQLALGQKPMTADDVLQYGADKVIIATGARWNTDGTNCLTHDPIPGADASLPDQLTPEQVMDGKKKIGKRVVILNADTYFMAPSLAEKLATAGHEVTIVSGVHLANYMHFTLEYPNMMRRLHELHVEELGDHFCSRIEPGRMEIYNIWGDGSKRTYRGPGVSPRDANTSHRWIEFDSLVLVTGRHSECTLWNELKARESEWAENDIKGIYLIGDAEAPRLIADATFTGHRVAREIEEANPQIAIPYKRETIAWGTPHMPGGNFKIEYKV

Entity 2 Entity 2 polymer

Description description	ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT
Molecular weight formula_weight	28929.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

MKILVAVKQTAALEEDFEIREDGMDVDEDFMMYDLNEWDDFSLEEAMKIKESSDTDVEVVVVSVGPDRVDESLRKCLAKGADRAVRVWDDAAEGSDAIVVGRILTEVIKKEAPDMVFAGVQSSDQAYASTGISVASYLNWPHAAVVADLQYKPGDNKAVIRRELEGGMLQEVEINCPAVLTIQLGINKPRYASLRGIKQAATKPIEEVSLADIGLSANDVGAAQSMSRVRRMYIPEKGRATMIEGTISEQAAKIIQIINEFKGA

Source Source

Source organism organism	METHYLOPHILUS METHYLOTROPHUS
NCBI taxonomy ID ncbi_taxonomy_id	17
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 polymer

Description description	ELECTRON TRANSFER FLAVOPROTEIN ALPHA-SUBUNIT
Molecular weight formula_weight	33622.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

SKILVIAEHRRNDLRPVSLELIGAANGLKKSGEDKVVVAVIGSQADAFVPALSVNGVDELVVVKGSSIDFDPDVFEASVSALIAAHNPSVVLLPHSVDSLGYASSLASKTGYGFATDVYIVEYQGDELVATRGGYNQKVNVEVDFPGKSTVVLTIRPSVFKPLEGAGSPVVSNVDAPSVQSRSQNKDYVEVGGGNDIDITTVDFIMSIGRGIGEETNVEQFRELADEAGATLCCSRPIADAGWLPKSRQVGQSGKVVGSCKLYVAMGISGSIQHMAGMKHVPTIIAVNTDPGASIFTIAKYGIVADIFDIEEELKAQLAA

Source Source

Source organism organism	METHYLOPHILUS METHYLOTROPHUS
NCBI taxonomy ID ncbi_taxonomy_id	17
Host organism host_organism	ESCHERICHIA COLI

Entity 4 Entity 4 non-polymer

Description description	FLAVIN MONONUCLEOTIDE
Molecular weight formula_weight	456.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 non-polymer

Description description	IRON/SULFUR CLUSTER
Molecular weight formula_weight	351.6 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 7 Entity 7 non-polymer

Description description	ADENOSINE MONOPHOSPHATE
Molecular weight formula_weight	347.2 kDa
Source method src_method	syn
Copy count entity_count	2

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6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

Domain ID domain_id	d1o95a1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.4 — FMN-linked oxidoreductases
Family Family family	c.1.4.1 — FMN-linked oxidoreductases

Domain ID domain_id	d1o95a2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamily	c.3.1 — FAD/NAD(P)-binding domain
Family Family family	c.3.1.1 — C-terminal domain of adrenodoxin reductase-like

Domain ID domain_id	d1o95a3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.4 — Nucleotide-binding domain
Superfamily Superfamily superfamily	c.4.1 — Nucleotide-binding domain
Family Family family	c.4.1.1 — N-terminal domain of adrenodoxin reductase-like

Domain ID domain_id	d1o95b1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.4 — FMN-linked oxidoreductases
Family Family family	c.1.4.1 — FMN-linked oxidoreductases

Domain ID domain_id	d1o95b2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamily	c.3.1 — FAD/NAD(P)-binding domain
Family Family family	c.3.1.1 — C-terminal domain of adrenodoxin reductase-like

Domain ID domain_id	d1o95b3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.4 — Nucleotide-binding domain
Superfamily Superfamily superfamily	c.4.1 — Nucleotide-binding domain
Family Family family	c.4.1.1 — N-terminal domain of adrenodoxin reductase-like

Domain ID domain_id	d1o95c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.26 — Adenine nucleotide alpha hydrolase-like
Superfamily Superfamily superfamily	c.26.2 — Adenine nucleotide alpha hydrolases-like
Family Family family	c.26.2.3 — ETFP subunits

Domain ID domain_id	d1o95d_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.26 — Adenine nucleotide alpha hydrolase-like
Superfamily Superfamily superfamily	c.26.2 — Adenine nucleotide alpha hydrolases-like
Family Family family	c.26.2.3 — ETFP subunits

Domain ID domain_id	d1o95e_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.26 — Adenine nucleotide alpha hydrolase-like
Superfamily Superfamily superfamily	c.26.2 — Adenine nucleotide alpha hydrolases-like
Family Family family	c.26.2.3 — ETFP subunits

Domain ID domain_id	d1o95f_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.26 — Adenine nucleotide alpha hydrolase-like
Superfamily Superfamily superfamily	c.26.2 — Adenine nucleotide alpha hydrolases-like
Family Family family	c.26.2.3 — ETFP subunits

CATH v4.4 (10 domains)

Domain ID domain_id	1o95A01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	1o95A02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

Domain ID domain_id	1o95A03
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	1o95B01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	1o95B02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

Domain ID domain_id	1o95B03
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	1o95C00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	620 — HUPs

Domain ID domain_id	1o95D00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	620 — HUPs

Domain ID domain_id	1o95E00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	620 — HUPs

Domain ID domain_id	1o95F00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	620 — HUPs

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Unit-cell length a length_a	102.500 Å
Unit-cell length b length_b	116.513 Å
Unit-cell length c length_c	138.706 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	95.35 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	3.700 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2570
R_work r_work	0.2520
R_free r_free	0.3530

Ternary complex between trimethylamine dehydrogenase and electron transferring flavoprotein

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

TRIMETHYLAMINE DEHYDROGENASE

State in the Current Structure

Other States of the Same Protein in the Database

ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

ELECTRON TRANSFER FLAVOPROTEIN ALPHA-SUBUNIT

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

1o95__assembly_1__model_1

1o95__assembly_1__model_1 | I(q)

1o95__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

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

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

CATH v4.4 (10 domains)

7. Citations (1)

Ternary complex between trimethylamine dehydrogenase and electron transferring flavoprotein

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

TRIMETHYLAMINE DEHYDROGENASE

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

ELECTRON TRANSFER FLAVOPROTEIN BETA-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

ELECTRON TRANSFER FLAVOPROTEIN ALPHA-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

1o95__assembly_1__model_1

1o95__assembly_1__model_1 | I(q)

1o95__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

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

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

CATH v4.4 (10 domains)

7. Citations (1)