SAXSdb — 1w6f

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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 homooligomer	Homooligomer	Protein 2	4-(DIAZENYLCARBONYL)PYRIDINE × 2 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	4-(DIAZENYLCARBONYL)PYRIDINE × 2 water × 2	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 4–278； UniProt 1–275 Author chain B； PDBConstruct 4–278； UniProt 1–275 Author chain C； PDBConstruct 4–278； UniProt 1–275 Author chain D； PDBConstruct 4–278； 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	1w6f
Deposition date deposition_date	2004-08-17
Structure title title	Arylamine N-acetyltransferase from Mycobacterium smegmatis with the anti-tubercular drug isoniazid bound in the active site.
Keywords keywords	NAT, TUBERCULOSIS, ACETYLTRANSFERASE, 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.

1w6f__assembly_1__model_1

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

Download this curve (.dat)

1w6f__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1w6f__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.66 Å
Rg (electron density)	29.21 Å
Total Rg	29.83 Å
Atom count	4230
Residues	542
Excluded volume	74245 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1w6f__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1w6f__assembly_2__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 (3)

Entity 1 Entity 1 polymer

Description description	ARYLAMINE N-ACETYLTRANSFERASE
Molecular weight formula_weight	30566.3 kDa
EC 编号 ec_number	2.3.1.5
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	9166

ESHMAMDLGGYLTRIGLDGRPRPDLGTLHAIVAAHNRSIPFENLDPLLGIPVADLSAEALFAKLVDRRRGGYCYEHNGLLGYVLEELGFEVERLSGRVVWMRADDAPLPAQTHNVLSVAVPGADGRYLVDVGFGGQTLTSPIRLEAGPVQQTRHEPYRLTRHGDDHTLAAQVRGEWQPLYTFTTEPRPRIDLEVGSWYVSTHPGSHFVTGLTVAVVTDDARYNLRGRNLAVHRSGATEHIRFDSAAQVLDAIVNRFGIDLGDLAGRDVQARVAEVLDT

Source Source

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

Entity 2 Entity 2 non-polymer

Description description	4-(DIAZENYLCARBONYL)PYRIDINE
Molecular weight formula_weight	135.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	718

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1w6fa_
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	d1w6fb_
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	d1w6fc_
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	d1w6fd_
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	1w6fA01
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	1w6fA02
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	1w6fB01
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	1w6fB02
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	1w6fC01
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	1w6fC02
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	1w6fD01
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	1w6fD02
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	101.208 Å
Unit-cell length b length_b	106.039 Å
Unit-cell length c length_c	140.362 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	2.100 Å
Low-resolution limit resolution_low	84.520 Å
R factor r_factor	0.1820
R_work r_work	0.1800
R_free r_free	0.2190

Arylamine N-acetyltransferase from Mycobacterium smegmatis with the anti-tubercular drug isoniazid bound in the active site.

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

1w6f__assembly_1__model_1

1w6f__assembly_1__model_1 | I(q)

1w6f__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (1)

Arylamine N-acetyltransferase from Mycobacterium smegmatis with the anti-tubercular drug isoniazid bound in the active site.

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

1w6f__assembly_1__model_1

1w6f__assembly_1__model_1 | I(q)

1w6f__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (1)