3dlx

Crystal structure of human 3-oxoacid CoA transferase 1

Method: X-RAY DIFFRACTION

▼

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

Succinyl-CoA:3-ketoacid-coenzyme A transferase 1

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	GLYCEROL × 1 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	GLYCEROL × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SCOT_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–482； UniProt 40–520 Author chain B； PDBConstruct 2–482； UniProt 40–520 Author chain C； PDBConstruct 2–482； UniProt 40–520 Author chain D； PDBConstruct 2–482； UniProt 40–520

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	3dlx
Deposition date deposition_date	2008-06-30
Structure title title	Crystal structure of human 3-oxoacid CoA transferase 1
Keywords keywords	;OXCT1, SCOT, Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, Disease mutation, Mitochondrion, Transit peptide, Structural Genomics, Structural Genomics Consortium, SGC, TRANSFERASE ;; TRANSFERASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

3dlx__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3dlx__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3dlx__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	29.50 Å
Rg (electron density)	28.72 Å
Total Rg	29.47 Å
Atom count	6874
Residues	926
Excluded volume	122810 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3dlx__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3dlx__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Succinyl-CoA:3-ketoacid-coenzyme A transferase 1
Molecular weight formula_weight	53150.8 kDa
EC 编号 ec_number	2.8.3.5
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	14234

MTKFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSPIKYNKDGSVAIASKPREVREFNGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEKYEKRIERLSIRKEGDGEAKSAKPGDDVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEADADLINAGKETVTILPGASFFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDKKKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQQIANAENLYFQ

Source Source

Source organism organism	Homo sapiens
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	375

▼

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d3dlxa1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.124 — NagB/RpiA/CoA transferase-like
Superfamily Superfamily superfamily	c.124.1 — NagB/RpiA/CoA transferase-like
Family Family family	c.124.1.2 — CoA transferase alpha subunit-like

Domain ID domain_id	d3dlxa2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.124 — NagB/RpiA/CoA transferase-like
Superfamily Superfamily superfamily	c.124.1 — NagB/RpiA/CoA transferase-like
Family Family family	c.124.1.3 — CoA transferase beta subunit-like

Domain ID domain_id	d3dlxb1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.124 — NagB/RpiA/CoA transferase-like
Superfamily Superfamily superfamily	c.124.1 — NagB/RpiA/CoA transferase-like
Family Family family	c.124.1.2 — CoA transferase alpha subunit-like

Domain ID domain_id	d3dlxb2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.124 — NagB/RpiA/CoA transferase-like
Superfamily Superfamily superfamily	c.124.1 — NagB/RpiA/CoA transferase-like
Family Family family	c.124.1.3 — CoA transferase beta subunit-like

Domain ID domain_id	d3dlxc1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.124 — NagB/RpiA/CoA transferase-like
Superfamily Superfamily superfamily	c.124.1 — NagB/RpiA/CoA transferase-like
Family Family family	c.124.1.2 — CoA transferase alpha subunit-like

Domain ID domain_id	d3dlxc2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.124 — NagB/RpiA/CoA transferase-like
Superfamily Superfamily superfamily	c.124.1 — NagB/RpiA/CoA transferase-like
Family Family family	c.124.1.3 — CoA transferase beta subunit-like

Domain ID domain_id	d3dlxd1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.124 — NagB/RpiA/CoA transferase-like
Superfamily Superfamily superfamily	c.124.1 — NagB/RpiA/CoA transferase-like
Family Family family	c.124.1.2 — CoA transferase alpha subunit-like

Domain ID domain_id	d3dlxd2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.124 — NagB/RpiA/CoA transferase-like
Superfamily Superfamily superfamily	c.124.1 — NagB/RpiA/CoA transferase-like
Family Family family	c.124.1.3 — CoA transferase beta subunit-like

CATH v4.4 (8 domains)

Domain ID domain_id	3dlxA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1080 — Glutaconate Coenzyme A-transferase
Homologous superfamily homologous superfamily	10 — Glutaconate Coenzyme A-transferase

Domain ID domain_id	3dlxA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1080 — Glutaconate Coenzyme A-transferase
Homologous superfamily homologous superfamily	10 — Glutaconate Coenzyme A-transferase

Domain ID domain_id	3dlxB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1080 — Glutaconate Coenzyme A-transferase
Homologous superfamily homologous superfamily	10 — Glutaconate Coenzyme A-transferase

Domain ID domain_id	3dlxB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1080 — Glutaconate Coenzyme A-transferase
Homologous superfamily homologous superfamily	10 — Glutaconate Coenzyme A-transferase

Domain ID domain_id	3dlxC01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1080 — Glutaconate Coenzyme A-transferase
Homologous superfamily homologous superfamily	10 — Glutaconate Coenzyme A-transferase

Domain ID domain_id	3dlxC02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1080 — Glutaconate Coenzyme A-transferase
Homologous superfamily homologous superfamily	10 — Glutaconate Coenzyme A-transferase

Domain ID domain_id	3dlxD01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1080 — Glutaconate Coenzyme A-transferase
Homologous superfamily homologous superfamily	10 — Glutaconate Coenzyme A-transferase

Domain ID domain_id	3dlxD02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1080 — Glutaconate Coenzyme A-transferase
Homologous superfamily homologous superfamily	10 — Glutaconate Coenzyme A-transferase

▶

Unit-cell length a length_a	60.956 Å
Unit-cell length b length_b	168.492 Å
Unit-cell length c length_c	95.322 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	105.86 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

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

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	48.110 Å
R factor r_factor	0.1789
R_work r_work	0.1782
R_free r_free	0.2247

Crystal structure of human 3-oxoacid CoA transferase 1

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

Succinyl-CoA:3-ketoacid-coenzyme A transferase 1

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

3dlx__assembly_2__model_1

3dlx__assembly_2__model_1 | I(q)

3dlx__assembly_2__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) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)

Crystal structure of human 3-oxoacid CoA transferase 1

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

Succinyl-CoA:3-ketoacid-coenzyme A transferase 1

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

3dlx__assembly_2__model_1

3dlx__assembly_2__model_1 | I(q)

3dlx__assembly_2__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) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)