1h5n

DMSO REDUCTASE MODIFIED BY THE PRESENCE OF DMS AND AIR

Method: X-RAY DIFFRACTION

▼

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

Dimethyl sulfoxide/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	2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE × 2 MOLYBDENUM(VI) ION × 1 SULFATE ION × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE × 2 MOLYBDENUM(VI) ION × 1 SULFATE ION × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DSTOR_RHOCA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–823； UniProt 1–823 Author chain C； PDBConstruct 1–823； UniProt 1–823

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1h5n
Deposition date deposition_date	2001-05-22
Structure title title	DMSO REDUCTASE MODIFIED BY THE PRESENCE OF DMS AND AIR
Keywords keywords	OXIDOREDUCTASE, REDUCTASE, DMSO, DMS, MOLYBDOPTERIN; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

1h5n__assembly_2__model_1

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

Download this curve (.dat)

1h5n__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1h5n__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	26.42 Å
Rg (electron density)	25.62 Å
Total Rg	26.47 Å
Atom count	5977
Residues	766
Excluded volume	105430 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1h5n__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1h5n__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Dimethyl sulfoxide/trimethylamine N-oxide reductase
Molecular weight formula_weight	89524.9 kDa
EC 编号 ec_number	1.7.2.3,1.8.5.3
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	13178

MTKFSGNELRAELYRRAFLSYSVAPGALGMFGRSLLAKGARAEALANGTVMSGSHWGVFTATVENGRATAFTPWEKDPHPSPMLAGVLDSIYSPTRIKYPMVRREFLEKGVNADRSTRGNGDFVRVSWDQALDLVAAEVKRVEETYGPEGVFGGSYGWKSPGRLHNCTTLLRRMLTLAGGYVNGAGDYSTGAAQVIMPHVVGTLEVYEQQTAWPVLAENTEVMVFWAADPIKTSQIGWVIPEHGAYPGLEALKAKGTKVIVIDPVRTKTVEFFGAEHITPKPQTDVAIMLGMAHTLVAEDLYDKDFIANYTSGFDKFLPYLDGETDSTPKTAEWAEGISGVPAETIKELARLFESKRTMLAAGWSMQRMHHGEQAHWMLVTLASMLGQIGLPGGGFGLSYHYSGGGTPSTSGPALAGITDGGAATKGPEWLAASGASVIPVARVVDMLENPGAEFDFNGTRSKFPDVKMAYWVGGNPFVHHQDRNRMVKAWEKLETFVVHDFQWTPTARHADIVLPATTSYERNDIETIGDYSNTGILAMKKIVEPLYEARSDYDIFAAVAERLGKGAEFTEGKDEMGWIKSFYDDAAKQGKAAGVQMPAFDAFWAEGIVEFPVTDGADFVRYASFREDPLLNPLGTPTGLIEIYSKNIEKMGYDDCPAHPTWMEPLERLDGPGAKYPLHIAASHPFNRLHSQLNGTVLREGYAVQGHEPCLMHPDDAAARGIADGDVVRVHNDRGQILTGVKVTDAVMKGVIQIYEGGWYDPSDVTEPGTLDKYGDVNVLSADIGTSKLAQGNCGQTVLAEVEKYTGPAVTLTGFVAPKAAE

Entity 2 Entity 2 non-polymer

Description description	2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE
Molecular weight formula_weight	738.5 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	MOLYBDENUM(VI) ION
Molecular weight formula_weight	95.9 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1234

▼

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1h5na1
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	d1h5na2
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

Domain ID domain_id	d1h5nc1
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	d1h5nc2
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 (8 domains)

Domain ID domain_id	1h5nA01
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	1h5nA02
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	1h5nA03
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	1h5nA04
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	40 — Barwin-like endoglucanases
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1h5nC01
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	1h5nC02
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	1h5nC03
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	1h5nC04
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	40 — Barwin-like endoglucanases
Homologous superfamily homologous superfamily	20 —

▶

Unit-cell length a length_a	68.800 Å
Unit-cell length b length_b	116.100 Å
Unit-cell length c length_c	230.400 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.1580
R_free r_free	0.2090

DMSO REDUCTASE MODIFIED BY THE PRESENCE OF DMS AND AIR

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

Dimethyl sulfoxide/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

1h5n__assembly_2__model_1

1h5n__assembly_2__model_1 | I(q)

1h5n__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (1)

DMSO REDUCTASE MODIFIED BY THE PRESENCE OF DMS AND AIR

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

Dimethyl sulfoxide/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

1h5n__assembly_2__model_1

1h5n__assembly_2__model_1 | I(q)

1h5n__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (1)