SAXSdb — 1gx3

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

ARYLAMINE N-ACETYLTRANSFERASE

MYCOBACTERIUM SMEGMATIS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
4	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	NAT_MYCSM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 10–284； UniProt 1–275 Author chain B； PDBConstruct 10–284； UniProt 1–275 Author chain C； PDBConstruct 10–284； UniProt 1–275 Author chain D； PDBConstruct 10–284； UniProt 1–275

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	1gx3
Deposition date deposition_date	2002-03-26
Structure title title	M. smegmatis arylamine N-acetyl transferase
Keywords keywords	TRANSFERASE, DRUG METABOLISM, MYCOBACTERIA, ISONIAZID, ARYLAMINE N- ACETYLTRANSFERASE, NAT; 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.

1gx3__assembly_1__model_1

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

Download this curve (.dat)

1gx3__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1gx3__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	19.16 Å
Rg (electron density)	17.86 Å
Total Rg	18.83 Å
Atom count	2136
Residues	276
Excluded volume	37540 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1gx3__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1gx3__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1gx3__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1gx3__assembly_4__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 (2)

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1gx3a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.3 — Cysteine proteinases
Superfamily Superfamily superfamily	d.3.1 — Cysteine proteinases
Family Family family	d.3.1.5 — Arylamine N-acetyltransferase

Domain ID domain_id	d1gx3b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.3 — Cysteine proteinases
Superfamily Superfamily superfamily	d.3.1 — Cysteine proteinases
Family Family family	d.3.1.5 — Arylamine N-acetyltransferase

Domain ID domain_id	d1gx3c_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.3 — Cysteine proteinases
Superfamily Superfamily superfamily	d.3.1 — Cysteine proteinases
Family Family family	d.3.1.5 — Arylamine N-acetyltransferase

Domain ID domain_id	d1gx3d_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.3 — Cysteine proteinases
Superfamily Superfamily superfamily	d.3.1 — Cysteine proteinases
Family Family family	d.3.1.5 — Arylamine N-acetyltransferase

CATH v4.4 (8 domains)

Domain ID domain_id	1gx3A01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2140 — Arylamine N-acetyltransferase fold
Homologous superfamily homologous superfamily	10 — Arylamine N-acetyltransferase

Domain ID domain_id	1gx3A02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	150 — Cysteine proteinases

Domain ID domain_id	1gx3B01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2140 — Arylamine N-acetyltransferase fold
Homologous superfamily homologous superfamily	10 — Arylamine N-acetyltransferase

Domain ID domain_id	1gx3B02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	150 — Cysteine proteinases

Domain ID domain_id	1gx3C01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2140 — Arylamine N-acetyltransferase fold
Homologous superfamily homologous superfamily	10 — Arylamine N-acetyltransferase

Domain ID domain_id	1gx3C02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	150 — Cysteine proteinases

Domain ID domain_id	1gx3D01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2140 — Arylamine N-acetyltransferase fold
Homologous superfamily homologous superfamily	10 — Arylamine N-acetyltransferase

Domain ID domain_id	1gx3D02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	150 — Cysteine proteinases

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Unit-cell length a length_a	101.250 Å
Unit-cell length b length_b	105.828 Å
Unit-cell length c length_c	141.320 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	16

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

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2110
R_work r_work	0.2090
R_free r_free	0.2410

Description description	ARYLAMINE N-ACETYLTRANSFERASE
Molecular weight formula_weight	31300.2 kDa
EC 编号 ec_number	2.3.1.5
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	9263

M. smegmatis arylamine N-acetyl transferase

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

ARYLAMINE N-ACETYLTRANSFERASE

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

1gx3__assembly_1__model_1

1gx3__assembly_1__model_1 | I(q)

1gx3__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (1)

Source organism organism	MYCOBACTERIUM SMEGMATIS
NCBI taxonomy ID ncbi_taxonomy_id	1772
Host organism host_organism	ESCHERICHIA COLI

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	755

M. smegmatis arylamine N-acetyl transferase

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

ARYLAMINE N-ACETYLTRANSFERASE

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

1gx3__assembly_1__model_1

1gx3__assembly_1__model_1 | I(q)

1gx3__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (1)