SAXSdb — 1tmo

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

TRIMETHYLAMINE N-OXIDE REDUCTASE

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	;GUANYLATE-O'-PHOSPHORIC ACID MONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,5,6,7,8A,9,10,10A-OCTAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL) ESTER ; × 2 MOLYBDENUM (IV)OXIDE × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TORA_SHEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–829； UniProt 1–829

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	1tmo
Deposition date deposition_date	1998-08-03
Structure title title	TRIMETHYLAMINE N-OXIDE REDUCTASE FROM SHEWANELLA MASSILIA
Keywords keywords	OXIDOREDUCTASE, TMAO REDUCTASE, OXOTRANSFERASE, MOLYBDOENZYME, MO-COFACTOR, MOLYBDENUM, BIS (MOLYBDOPTERIN GUANINE DINUCLEOTIDE); 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.

1tmo__assembly_1__model_1

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

Download this curve (.dat)

1tmo__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1tmo__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	27.68 Å
Rg (electron density)	26.95 Å
Total Rg	27.81 Å
Atom count	6352
Residues	794
Excluded volume	112100 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1tmo__assembly_1__model_1`	monomeric （1）	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	TRIMETHYLAMINE N-OXIDE REDUCTASE
Molecular weight formula_weight	92476.9 kDa
EC 编号 ec_number	1.6.6.9
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	6857

MNRRDFLKGIASSSFVVLGGSSVLTPLNALAKAGINEDEWLTTGSHFGAFKMKRKNGVIAEVKPFDLDKYPTDMINGIRGMVYNPSRVRYPMVRLDFLLKGHKSNTHQRGDFRFVRVTWDKALTLFKHSLDEVQTQYGPSGLHAGQTGWRATGQLHSSTSHMQRAVGMHGNYVKKIGDYSTGAGQTILPYVLGSTEVYAQGTSWPLILEHSDTIVLWSNDPYKNLQVGWNAETHESFAYLAQLKEKVKQGKIRVISIDPVVTKTQAYLGCEQLYVNPQTDVTLMLAIAHEMISKKLYDDKFIQGYSLGFEEFVPYVMGTKDGVAKTPEWAAPICGVEAHVIRDLAKTLVKGRTQFMMGWCIQRQQHGEQPYWMAAVLATMIGQIGLPGGGISYGHHYSSIGVPSSGAAAPGAFPRNLDENQKPLFDSSDFKGASSTIPVARWIDAILEPGKTIDANGSKVVYPDIKMMIFSGNNPWNHHQDRNRMKQAFHKLECVVTVDVNWTATCRFSDIVLPACTTYERNDIDVYGAYANRGILAMQKMVEPLFDSLSDFEIFTRFAAVLGKEKEYTRNMGEMEWLETLYNECKAANAGKFEMPDFATFWKQGYVHFGDGEVWTRHADFRNDPEINPLGTPSGLIEIFSRKIDQFGYDDCKGHPTWMEKTERSHGGPGSDKHPIWLQSCHPDKRLHSQMCESREYRETYAVNGREPVYISPVDAKARGIKDGDIVRVFNDRGQLLAGAVVSDNFPKGIVRIHEGAWYGPVGKDGSTEGGAEVGALCSYGDPNTLTLDIGTSKLAQACSAYTCLVEFEKYQGKVPKVSSFDGPIEVEI

Entity 2 Entity 2 non-polymer

Description description	;GUANYLATE-O'-PHOSPHORIC ACID MONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,5,6,7,8A,9,10,10A-OCTAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL) ESTER ;
Molecular weight formula_weight	742.6 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	MOLYBDENUM (IV)OXIDE
Molecular weight formula_weight	127.9 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	505

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1tmoa1
Class class	b — All beta proteins
Fold Fold fold	b.52 — Double psi beta-barrel
Superfamily Superfamily superfamily	b.52.2 — ADC-like
Family Family family	b.52.2.2 — Formate dehydrogenase/DMSO reductase, C-terminal domain

Domain ID domain_id	d1tmoa2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.81 — Formate dehydrogenase/DMSO reductase, domains 1-3
Superfamily Superfamily superfamily	c.81.1 — Formate dehydrogenase/DMSO reductase, domains 1-3
Family Family family	c.81.1.1 — Formate dehydrogenase/DMSO reductase, domains 1-3

CATH v4.4 (4 domains)

Domain ID domain_id	1tmoA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	740 —

Domain ID domain_id	1tmoA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	228 — Dimethylsulfoxide Reductase; domain 2
Homologous superfamily homologous superfamily	10 — Dimethylsulfoxide Reductase, domain 2

Domain ID domain_id	1tmoA03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	55 — Dimethylsulfoxide Reductase; domain 3
Homologous superfamily homologous superfamily	10 — Dimethylsulfoxide Reductase, domain 3

Domain ID domain_id	1tmoA04
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	40 — Barwin-like endoglucanases
Homologous superfamily homologous superfamily	20 —

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Unit-cell length a length_a	123.320 Å
Unit-cell length b length_b	140.700 Å
Unit-cell length c length_c	59.390 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1820
R_work r_work	0.1820
R_free r_free	0.2470

TRIMETHYLAMINE N-OXIDE REDUCTASE FROM SHEWANELLA MASSILIA

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

TRIMETHYLAMINE N-OXIDE REDUCTASE

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

1tmo__assembly_1__model_1

1tmo__assembly_1__model_1 | I(q)

1tmo__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (2)

TRIMETHYLAMINE N-OXIDE REDUCTASE FROM SHEWANELLA MASSILIA

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

TRIMETHYLAMINE N-OXIDE REDUCTASE

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

1tmo__assembly_1__model_1

1tmo__assembly_1__model_1 | I(q)

1tmo__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (2)