SAXSdb — 1m6y

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

S-adenosyl-methyltransferase mraW

Thermotoga maritima

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	SULFATE ION × 1 S-ADENOSYL-L-HOMOCYSTEINE × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	SULFATE ION × 1 S-ADENOSYL-L-HOMOCYSTEINE × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MRAW_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–301； UniProt 1–299 Author chain B； PDBConstruct 3–301； UniProt 1–299

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	1m6y
Deposition date deposition_date	2002-07-17
Structure title title	Crystal Structure Analysis of TM0872, a Putative SAM-dependent Methyltransferase, Complexed with SAH
Keywords keywords	;SAM-dependent Methyltransferase Fold, Protein-Cofactor Product Complex, Structural Genomics, PSI, Protein Structure Initiative, Midwest Center for Structural Genomics, MCSG, TRANSFERASE ;; TRANSFERASE
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.

1m6y__assembly_1__model_1

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

Download this curve (.dat)

1m6y__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1m6y__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	20.37 Å
Rg (electron density)	19.46 Å
Total Rg	20.25 Å
Atom count	2436
Residues	289
Excluded volume	43515 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1m6y__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1m6y__assembly_2__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	S-adenosyl-methyltransferase mraW
Molecular weight formula_weight	35385.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5064

GHMRKYSQRHIPVMVREVIEFLKPEDEKIILDCTVGEGGHSRAILEHCPGCRIIGIDVDSEVLRIAEEKLKEFSDRVSLFKVSYREADFLLKTLGIEKVDGILMDLGVSTYQLKGENRGFTFEREEPLDMRMDLESEVTAQKVLNELPEEELARIIFEYGEEKRFARRIARKIVENRPLNTTLDLVKAVREALPSYEIRRRKRHFATKTFQAIRIYVNRELENLKEFLKKAEDLLNPGGRIVVISFHSLEDRIVKETFRNSKKLRILTEKPVRPSEEEIRENPRARSGRLRAAERIEEGGD

Source Source

Source organism organism	Thermotoga maritima
NCBI taxonomy ID ncbi_taxonomy_id	2336
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

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

Entity 3 Entity 3 non-polymer

Description description	S-ADENOSYL-L-HOMOCYSTEINE
Molecular weight formula_weight	384.4 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	367

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1m6ya1
Class class	a — All alpha proteins
Fold Fold fold	a.60 — SAM domain-like
Superfamily Superfamily superfamily	a.60.13 — Putative methyltransferase TM0872, insert domain
Family Family family	a.60.13.1 — Putative methyltransferase TM0872, insert domain

Domain ID domain_id	d1m6ya2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.66 — S-adenosyl-L-methionine-dependent methyltransferases
Superfamily Superfamily superfamily	c.66.1 — S-adenosyl-L-methionine-dependent methyltransferases
Family Family family	c.66.1.23 — MraW-like putative methyltransferases

Domain ID domain_id	d1m6yb1
Class class	a — All alpha proteins
Fold Fold fold	a.60 — SAM domain-like
Superfamily Superfamily superfamily	a.60.13 — Putative methyltransferase TM0872, insert domain
Family Family family	a.60.13.1 — Putative methyltransferase TM0872, insert domain

Domain ID domain_id	d1m6yb2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.66 — S-adenosyl-L-methionine-dependent methyltransferases
Superfamily Superfamily superfamily	c.66.1 — S-adenosyl-L-methionine-dependent methyltransferases
Family Family family	c.66.1.23 — MraW-like putative methyltransferases

CATH v4.4 (4 domains)

Domain ID domain_id	1m6yA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	150 — Vaccinia Virus protein VP39

Domain ID domain_id	1m6yA02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily	170 — Putative methyltransferase TM0872, insert domain

Domain ID domain_id	1m6yB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	150 — Vaccinia Virus protein VP39

Domain ID domain_id	1m6yB02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily	170 — Putative methyltransferase TM0872, insert domain

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Unit-cell length a length_a	133.400 Å
Unit-cell length b length_b	133.400 Å
Unit-cell length c length_c	133.400 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	24

Space group space_group	P 21 3
Space-group number int_tables_number	198
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	19.890 Å
R factor r_factor	—
R_work r_work	0.1970
R_free r_free	0.2120

Crystal Structure Analysis of TM0872, a Putative SAM-dependent Methyltransferase, Complexed with SAH

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

S-adenosyl-methyltransferase mraW

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

1m6y__assembly_1__model_1

1m6y__assembly_1__model_1 | I(q)

1m6y__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

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Crystal Structure Analysis of TM0872, a Putative SAM-dependent Methyltransferase, Complexed with SAH

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

S-adenosyl-methyltransferase mraW

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

1m6y__assembly_1__model_1

1m6y__assembly_1__model_1 | I(q)

1m6y__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

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)