SAXSdb — 9tqc

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

Propionyl CoA carboxylase beta subunit

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 10	Biotin carboxylase × 4 （Q5ZUG9） 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q5ZUH1_LEGPH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–535； UniProt 1–535 Author chain B； PDBConstruct 1–535； UniProt 1–535 Author chain C； PDBConstruct 1–535； UniProt 1–535 Author chain D； PDBConstruct 1–535； UniProt 1–535 Author chain E； PDBConstruct 1–535； UniProt 1–535 Author chain F； PDBConstruct 1–535； UniProt 1–535

Biotin carboxylase

OrganismNot specified

UniProt Q5ZUG9

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 10	Propionyl CoA carboxylase beta subunit × 6 （Q5ZUH1） 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q5ZUG9_LEGPH
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain G； PDBConstruct 1–677； UniProt 1–677 Author chain H； PDBConstruct 1–677； UniProt 1–677 Author chain I； PDBConstruct 1–677； UniProt 1–677 Author chain J； PDBConstruct 1–677； UniProt 1–677

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	9tqc
Deposition date deposition_date	2025-12-19
Structure title title	L. pneumophila 3-methylcrotonyl-CoA carboxylase holoenzyme A3B6
Keywords keywords	3-methylcrotonyl-CoA carboxylase, ligase, biotin; LIGASE
Experimental Method method	ELECTRON MICROSCOPY

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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.

9tqc__assembly_1__model_1

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

Download this curve (.dat)

9tqc__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9tqc__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	57.00 Å
Rg (electron density)	56.47 Å
Total Rg	56.73 Å
Atom count	40135
Residues	5149
Excluded volume	715430 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9tqc__assembly_1__model_1`	decameric （10）	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 beta subunit
Molecular weight formula_weight	58525.6 kDa
EC 编号 ec_number	6.4.1.3
Source method src_method	nat
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	40135

MAKLTTQINTSSQEFKNNQANMQALVTDLREKIHQISLGGDEKARTKHQQQGKLLPRERLHQLLDPGSPFLELSQLAAYQVYEDTIPAAGIITGIGRVAGNECVIVVNDATVKGGTYYPLTVKKHLRAQEIALINHLPCIYLVDSGGAFLPLQDQVFADKEHFGRVFYNQAQMSALNIPQIAVVMGSCTAGGAYVPAMADESIMVKNQATIFLGGPPLVKAATGEVISAEELGGAEVHCRHSGVSDHYAENDAHALHLARVAISNLNRKKPDSIHRVDTVPPLYDSEDLTGIIPTDPRKPFDIREIIARVVDGSEFDEFKALFGTTLVCGFARLYGYPIGIIANNGILFSESAQKGSHFIELCCQRKIPLVFLQNITGFMVGSKYEASGIAKHGAKMVTAVANANVPKFTIIVGGSFGAGNYAMCGRAYAPRFLWAWPNARISVMGGEQAANVLAQITREKYAKQGKEWSLEEEEQFKTQMRSQYETQGNPYYASARLWDDGVIAPQDTRKILGLGLSAALNAPIEDTRFGVFRM

Entity 2 Entity 2 polymer

Description description	Biotin carboxylase
Molecular weight formula_weight	75811.0 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,J,H,I

MRGKKGLKHFSIKKYPTGIKVLDMFNKILIANRGEIACRIIKTAHSMGIQAIAVYSAADRNSLHVRLADSAYYIGEAPAKESYLNIDHIIQAAKESGAQAIHPGYGFLSENPDFAKACEQAGIVFIGPSIKAMEAMASKQLAKQLLEKTKVPLTPGYHGVEQSEEKLLSEAKKIGFPVLIKAANGGGGKGMRAVHDEKEFHDALAGAKRESMASFADDTMIIERLVLNPRHVEVQIMADNHGNVVNLFERDCSIQRRHQKIIEEAPAPNLLPVLRQRLAEAACEVARSINYRGAGTVEFLVDGEDKFYFMEMNTRLQVEHPVTEMITGLDLVAWQIKIAANDTLPLLQNQIQAQGHAIECRIYAEDPYQGFIPSIGQLQFLKEPSGDGIRIDTGVTLSSEITRYYDPMIAKLIAWGHNREEALHRLERSLAHYDIGGVKTNIPFLRAICQHVKFKEAKLSTDFLEKENISLPKPDNELGMLLAISYDYLGMINRTTDPLLQEAFGWQMHLSSHWIWRYQLNSTIIEAQITPIDNKKFKAKIENKEMVIYARYDIDQLIIEIDQKSVKARVENKDHHLIFYTDKGQLSIERFYWSKLDAQTSAHKGQLTAPMPATVVAILKNIGEQVKAGESLIVLEAMKMEHTIHAPIDGILSDIFYSVGSQVSEGAELLALSESDT

Entity 3 Entity 3 non-polymer

Description description	5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL
Molecular weight formula_weight	228.3 kDa
Source method src_method	syn
Copy count entity_count	6

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

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

Resolution resolution	2.480 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

L. pneumophila 3-methylcrotonyl-CoA carboxylase holoenzyme A3B6

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

Propionyl CoA carboxylase beta subunit

State in the Current Structure

Other States of the Same Protein in the Database

Biotin carboxylase

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

9tqc__assembly_1__model_1

9tqc__assembly_1__model_1 | I(q)

9tqc__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

7. Citations (1)

L. pneumophila 3-methylcrotonyl-CoA carboxylase holoenzyme A3B6

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

Propionyl CoA carboxylase beta subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Biotin carboxylase

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

9tqc__assembly_1__model_1

9tqc__assembly_1__model_1 | I(q)

9tqc__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

7. Citations (1)