SAXSdb — 1xa4

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

Crotonobetainyl-CoA:carnitine CoA-transferase

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	SULFATE ION × 1 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 COENZYME A × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CAIB_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 26–429； UniProt 2–405 Author chain B； PDBConstruct 26–429； UniProt 2–405

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	1xa4
Deposition date deposition_date	2004-08-25
Structure title title	Crystal structure of CaiB, a type III CoA transferase in carnitine metabolism
Keywords keywords	CaiB, carnitine, CoA transferase, CoA, Coenzyme A, interlocked, dimer, Bis-tris, 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.

1xa4__assembly_1__model_1

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

Download this curve (.dat)

1xa4__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1xa4__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	27.12 Å
Rg (electron density)	26.24 Å
Total Rg	26.81 Å
Atom count	6335
Residues	768
Excluded volume	113590 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1xa4__assembly_1__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 (5)

Entity 1 Entity 1 polymer

Description description	Crotonobetainyl-CoA:carnitine CoA-transferase
Molecular weight formula_weight	49700.8 kDa
EC 编号 ec_number	2.8.3.-
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	6910

MHHHHHHGSTSLYKKAGSETLYIQGDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQLSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVIAHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAALAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYKCADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWLATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKFKNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVEDSTHHHHHH

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
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	1

Entity 3 Entity 3 non-polymer

Description description	2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
Molecular weight formula_weight	209.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	COENZYME A
Molecular weight formula_weight	767.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	575

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1xa4a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.123 — CoA-transferase family III (CaiB/BaiF)
Superfamily Superfamily superfamily	c.123.1 — CoA-transferase family III (CaiB/BaiF)
Family Family family	c.123.1.1 — CoA-transferase family III (CaiB/BaiF)

Domain ID domain_id	d1xa4b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.123 — CoA-transferase family III (CaiB/BaiF)
Superfamily Superfamily superfamily	c.123.1 — CoA-transferase family III (CaiB/BaiF)
Family Family family	c.123.1.1 — CoA-transferase family III (CaiB/BaiF)

CATH v4.4 (4 domains)

Domain ID domain_id	1xa4A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10540 — Crotonobetainyl-coa:carnitine coa-transferase; domain 1

Domain ID domain_id	1xa4A02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1540 — formyl-coa transferase, domain 3
Homologous superfamily homologous superfamily	10 — formyl-coa transferase, domain 3

Domain ID domain_id	1xa4B01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10540 — Crotonobetainyl-coa:carnitine coa-transferase; domain 1

Domain ID domain_id	1xa4B02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1540 — formyl-coa transferase, domain 3
Homologous superfamily homologous superfamily	10 — formyl-coa transferase, domain 3

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Unit-cell length a length_a	55.595 Å
Unit-cell length b length_b	125.668 Å
Unit-cell length c length_c	69.963 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	108.96 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.1453
R_work r_work	0.1436
R_free r_free	0.1755

Crystal structure of CaiB, a type III CoA transferase in carnitine metabolism

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

Crotonobetainyl-CoA:carnitine CoA-transferase

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

1xa4__assembly_1__model_1

1xa4__assembly_1__model_1 | I(q)

1xa4__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 (5)

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 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Crystal structure of CaiB, a type III CoA transferase in carnitine metabolism

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

Crotonobetainyl-CoA:carnitine CoA-transferase

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

1xa4__assembly_1__model_1

1xa4__assembly_1__model_1 | I(q)

1xa4__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 (5)

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 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)