SAXSdb — 2h3w

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

carnitine acetyltransferase

Mus musculus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	COENZYME A × 1 (R)-3-CARBOXY-2-(HEXANOYLOXY)-N,N,N-TRIMETHYLPROPAN-1-AMINIUM × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	COENZYME A × 1 (R)-3-CARBOXY-2-(HEXANOYLOXY)-N,N,N-TRIMETHYLPROPAN-1-AMINIUM × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q3V1Y3_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–599； UniProt 30–625 Author chain B； PDBConstruct 4–599； UniProt 30–625

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	2h3w
Deposition date deposition_date	2006-05-23
Structure title title	Crystal structure of the S554A/M564G mutant of murine carnitine acetyltransferase in complex with hexanoylcarnitine and CoA
Keywords keywords	carnitine acyltransferase, 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.

2h3w__assembly_1__model_1

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

Download this curve (.dat)

2h3w__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2h3w__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	25.87 Å
Rg (electron density)	24.89 Å
Total Rg	25.76 Å
Atom count	4842
Residues	599
Excluded volume	86328 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2h3w__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2h3w__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	carnitine acetyltransferase
Molecular weight formula_weight	67947.7 kDa
Mutation mutation	S554A:M564G
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	11184

SHMAHQDALPRLPVPPLQQSLDYYLKALQPIVSEEEWAHTKQLVDEFQTSGGVGERLQKGLERRAKKMENWLSEWWLKTAYLQFRQPVVIYSSPGVILPKQDFVDLQGQLRFAAKLIEGVLDFKSMIDNETLPVEFLGGQPLCMNQYYQILSSCRVPGPKQDSVVNFLKSKRPPTHITVVHNYQFFELDVYHSDGTPLTSDQIFVQLEKIWNSSLQSNKEPVGILTSNHRNTWAKAYNNLIKDKVNRESVNSIQKSIFTVCLDKQVPRVSDDVYRNHVAGQMLHGGGSKFNSGNRWFDKTLQFIVAEDGSCGMVYEHAAAEGPPIVALVDHVMEYTKKPELVRSPMVPLPMPKKLRFNITPEIKNDIEKAKQNLSIMIQDLDIMMLTFHHFGKDFPKSEKLSPDAFIQVALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASIDSLAFVKGMGDSTVPEQQKVELLRKAVQAHRAYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMDTSYAIAMHFNLSTAQVPAKTDCVGFFGPVVPDGYGICYNPMEAHINFSVSAYNSCAETNAARMAHYLEKALLDMRTLLQNHPRAK

Source Source

Source organism organism	Mus musculus
Common name common_name	house mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	COENZYME A
Molecular weight formula_weight	767.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	(R)-3-CARBOXY-2-(HEXANOYLOXY)-N,N,N-TRIMETHYLPROPAN-1-AMINIUM
Molecular weight formula_weight	260.4 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	1500

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d2h3wa1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.43 — CoA-dependent acyltransferases
Superfamily Superfamily superfamily	c.43.1 — CoA-dependent acyltransferases
Family Family family	c.43.1.3 — Choline/Carnitine O-acyltransferase

Domain ID domain_id	d2h3wa2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.43 — CoA-dependent acyltransferases
Superfamily Superfamily superfamily	c.43.1 — CoA-dependent acyltransferases
Family Family family	c.43.1.3 — Choline/Carnitine O-acyltransferase

Domain ID domain_id	d2h3wa3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2h3wb1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.43 — CoA-dependent acyltransferases
Superfamily Superfamily superfamily	c.43.1 — CoA-dependent acyltransferases
Family Family family	c.43.1.3 — Choline/Carnitine O-acyltransferase

Domain ID domain_id	d2h3wb2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.43 — CoA-dependent acyltransferases
Superfamily Superfamily superfamily	c.43.1 — CoA-dependent acyltransferases
Family Family family	c.43.1.3 — Choline/Carnitine O-acyltransferase

Domain ID domain_id	d2h3wb3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (4 domains)

Domain ID domain_id	2h3wA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	559 — Chloramphenicol Acetyltransferase
Homologous superfamily homologous superfamily	10 — Chloramphenicol acetyltransferase-like domain

Domain ID domain_id	2h3wA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	559 — Chloramphenicol Acetyltransferase
Homologous superfamily homologous superfamily	70 — Choline/Carnitine o-acyltransferase, domain 2

Domain ID domain_id	2h3wB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	559 — Chloramphenicol Acetyltransferase
Homologous superfamily homologous superfamily	10 — Chloramphenicol acetyltransferase-like domain

Domain ID domain_id	2h3wB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	559 — Chloramphenicol Acetyltransferase
Homologous superfamily homologous superfamily	70 — Choline/Carnitine o-acyltransferase, domain 2

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Unit-cell length a length_a	164.060 Å
Unit-cell length b length_b	89.070 Å
Unit-cell length c length_c	122.780 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	128.97 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	29.910 Å
R factor r_factor	0.1770
R_work r_work	0.1770
R_free r_free	0.2190

Crystal structure of the S554A/M564G mutant of murine carnitine acetyltransferase in complex with hexanoylcarnitine and CoA

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

carnitine 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

2h3w__assembly_1__model_1

2h3w__assembly_1__model_1 | I(q)

2h3w__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) 10 domains

SCOP 2.08 (6 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Crystal structure of the S554A/M564G mutant of murine carnitine acetyltransferase in complex with hexanoylcarnitine and CoA

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

carnitine 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

2h3w__assembly_1__model_1

2h3w__assembly_1__model_1 | I(q)

2h3w__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) 10 domains

SCOP 2.08 (6 domains)

CATH v4.4 (4 domains)

7. Citations (1)