SAXSdb — 2jku

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

PROPIONYL-COA CARBOXYLASE ALPHA CHAIN, MITOCHONDRIAL

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	TETRAETHYLENE GLYCOL × 4 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PCCA_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 24–94； UniProt 633–703

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	2jku
Deposition date deposition_date	2008-08-30
Structure title title	Crystal structure of the N-terminal region of the biotin acceptor domain of human propionyl-CoA carboxylase
Keywords keywords	LIGASE, BIOTIN, ATP-BINDING, DISEASE MUTATION, NUCLEOTIDE-BINDING, MITOCHONDRION, PHOSPHOPROTEIN, TRANSIT PEPTIDE; LIGASE
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.

2jku__assembly_1__model_1

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

Download this curve (.dat)

2jku__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2jku__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	12.58 Å
Rg (electron density)	11.30 Å
Total Rg	12.76 Å
Atom count	530
Residues	70
Excluded volume	9690 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2jku__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 (3)

Entity 1 Entity 1 polymer

Description description	PROPIONYL-COA CARBOXYLASE ALPHA CHAIN, MITOCHONDRIAL
Molecular weight formula_weight	9940.2 kDa
EC 编号 ec_number	6.4.1.3
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	336

MHHHHHHSSGVDLGTENLYFQSMTSSVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE

Source Source

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	TETRAETHYLENE GLYCOL
Molecular weight formula_weight	194.2 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	58

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Unit-cell length a length_a	56.107 Å
Unit-cell length b length_b	56.107 Å
Unit-cell length c length_c	58.083 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 64 2 2
Space-group number int_tables_number	181
Crystal system crystal_system	—

Resolution resolution	1.500 Å
Low-resolution limit resolution_low	28.120 Å
R factor r_factor	0.1490
R_work r_work	0.1480
R_free r_free	0.1660

Crystal structure of the N-terminal region of the biotin acceptor domain of human propionyl-CoA carboxylase

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

PROPIONYL-COA CARBOXYLASE ALPHA CHAIN, MITOCHONDRIAL

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

2jku__assembly_1__model_1

2jku__assembly_1__model_1 | I(q)

2jku__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

7. Citations (1)

Crystal structure of the N-terminal region of the biotin acceptor domain of human propionyl-CoA carboxylase

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

PROPIONYL-COA CARBOXYLASE ALPHA CHAIN, MITOCHONDRIAL

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

2jku__assembly_1__model_1

2jku__assembly_1__model_1 | I(q)

2jku__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

7. Citations (1)