1g6q

CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1

Method: X-RAY DIFFRACTION

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

HNRNP ARGININE N-METHYLTRANSFERASE

Saccharomyces cerevisiae

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 6	No other associated polymer	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HMT1_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 1–328； UniProt 21–348 Author chain 2； PDBConstruct 1–328； UniProt 21–348 Author chain 3； PDBConstruct 1–328； UniProt 21–348 Author chain 4； PDBConstruct 1–328； UniProt 21–348 Author chain 5； PDBConstruct 1–328； UniProt 21–348 Author chain 6； PDBConstruct 1–328； UniProt 21–348

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	1g6q
Deposition date deposition_date	2000-11-07
Structure title title	CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1
Keywords keywords	SAM-binding domain, beta-barrel, mixed alpha-beta, hexamer, dimer, 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.

1g6q__assembly_4__model_1

Assembly 4 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1g6q__assembly_4__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1g6q__assembly_4__model_1 | P(r) · Pending

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

Rg（Guinier）	29.64 Å
Rg (electron density)	28.61 Å
Total Rg	29.42 Å
Atom count	5119
Residues	637
Excluded volume	91382 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1g6q__assembly_1__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1g6q__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1g6q__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1g6q__assembly_4__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 (1)

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6. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1g6q1_
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.66.1.6 — Arginine methyltransferase

Domain ID domain_id	d1g6q2_
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.66.1.6 — Arginine methyltransferase

Domain ID domain_id	d1g6q3_
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.66.1.6 — Arginine methyltransferase

Domain ID domain_id	d1g6q4_
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.66.1.6 — Arginine methyltransferase

Domain ID domain_id	d1g6q5_
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.66.1.6 — Arginine methyltransferase

Domain ID domain_id	d1g6q6_
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.66.1.6 — Arginine methyltransferase

CATH v4.4 (12 domains)

Domain ID domain_id	1g6q101
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	1g6q102
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	160 — Hnrnp arginine n-methyltransferase1
Homologous superfamily homologous superfamily	11 — Hnrnp arginine n-methyltransferase1

Domain ID domain_id	1g6q201
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	1g6q202
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	160 — Hnrnp arginine n-methyltransferase1
Homologous superfamily homologous superfamily	11 — Hnrnp arginine n-methyltransferase1

Domain ID domain_id	1g6q301
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	1g6q302
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	160 — Hnrnp arginine n-methyltransferase1
Homologous superfamily homologous superfamily	11 — Hnrnp arginine n-methyltransferase1

Domain ID domain_id	1g6q401
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	1g6q402
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	160 — Hnrnp arginine n-methyltransferase1
Homologous superfamily homologous superfamily	11 — Hnrnp arginine n-methyltransferase1

Domain ID domain_id	1g6q501
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	1g6q502
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	160 — Hnrnp arginine n-methyltransferase1
Homologous superfamily homologous superfamily	11 — Hnrnp arginine n-methyltransferase1

Domain ID domain_id	1g6q601
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	1g6q602
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	160 — Hnrnp arginine n-methyltransferase1
Homologous superfamily homologous superfamily	11 — Hnrnp arginine n-methyltransferase1

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Unit-cell length a length_a	84.100 Å
Unit-cell length b length_b	129.430 Å
Unit-cell length c length_c	101.430 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	102.74 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

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

Resolution resolution	2.900 Å
Low-resolution limit resolution_low	28.000 Å
R factor r_factor	0.2530
R_work r_work	0.2530
R_free r_free	0.2940

Description description	HNRNP ARGININE N-METHYLTRANSFERASE
Molecular weight formula_weight	37692.6 kDa
EC 编号 ec_number	2.1.1.-
Mutation mutation	Q21D, H22Y, N25D
Source method src_method	man
Copy count entity_count	6

Polymer type type	polypeptide(L)
Chain IDs strand_id	1,2,3,4,5,6
Atom count atom_count	15520

CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1

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

HNRNP ARGININE N-METHYLTRANSFERASE

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

1g6q__assembly_4__model_1

1g6q__assembly_4__model_1 | I(q)

1g6q__assembly_4__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (6 domains)

CATH v4.4 (12 domains)

7. Citations (5)

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	Escherichia coli

CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1

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

HNRNP ARGININE N-METHYLTRANSFERASE

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

1g6q__assembly_4__model_1

1g6q__assembly_4__model_1 | I(q)

1g6q__assembly_4__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (6 domains)

CATH v4.4 (12 domains)

7. Citations (5)