SAXSdb — 9yx0

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

Carboxyl transferase domain protein

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 12	biotin carboxylase × 6 （A0R1D8） BIOTIN × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0R1D9_MYCS2
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain G； PDBConstruct 1–513； UniProt 1–513 Author chain H； PDBConstruct 1–513； UniProt 1–513 Author chain I； PDBConstruct 1–513； UniProt 1–513 Author chain J； PDBConstruct 1–513； UniProt 1–513 Author chain K； PDBConstruct 1–513； UniProt 1–513 Author chain L； PDBConstruct 1–513； UniProt 1–513

biotin carboxylase

OrganismNot specified

UniProt A0R1D8

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 12	Carboxyl transferase domain protein × 6 （A0R1D9） BIOTIN × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0R1D8_MYCS2
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 1–669； UniProt 1–669 Author chain B； PDBConstruct 1–669； UniProt 1–669 Author chain C； PDBConstruct 1–669； UniProt 1–669 Author chain D； PDBConstruct 1–669； UniProt 1–669 Author chain E； PDBConstruct 1–669； UniProt 1–669 Author chain F； PDBConstruct 1–669； UniProt 1–669

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	9yx0
Deposition date deposition_date	2025-10-26
Structure title title	Structure of the 3-methylcrotonyl-coenzyme A carboxylase from Mycobacterium smegmatis
Keywords keywords	Carboxylase, transferase, leucine catabolism, metabolism, LIGASE; 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.

9yx0__assembly_1__model_1

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

Download this curve (.dat)

9yx0__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9yx0__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	62.44 Å
Rg (electron density)	62.27 Å
Total Rg	62.23 Å
Atom count	47381
Residues	6588
Excluded volume	838680 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9yx0__assembly_1__model_1`	12-meric （12）	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	Carboxyl transferase domain protein
Molecular weight formula_weight	54816.2 kDa
Source method src_method	nat
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,H,I,J,K,L
Atom count atom_count	47381

MSSHRDEHLALVAELRSKLAAAALGGPERARERHVGRGKLLPRDRVDGLLDPGSPFLELAPLAAGGMYDDECPGAGMIAGIGRVSGRECVIVANDATVKGGTYYPITVKKHLRAQEIALQNKLPCIYLVDSGGAFLPRQDEVFPDRDHFGRIFYNQATMSAQGIAQIAAVLGSCTAGGAYVPAMSDEAVIVRNQGTIFLGGPPLVKAATGEVVTAEELGGGDLHSKTSGVTDHLAHDDRDALRIVRNIVATLGPAEPPPWQVLPAVDPIADQTELYDVVPVDARVPYDVHEVITRIVDGGEFGEFKAEYGTTLVTGFARIHGHPVGIIANNGVLFGESAVKGAHFIELCDKRKTPLLFLQNISGFMVGRDYEAGGIAKHGAKMVTAVACARVPKLTVVIGGSYGAGNYSMCGRAYSPRFLWMWPNARISVMGGEQAASVLATVRGEMTDAEAEEFKAPIREQYEHQGNPYYSTARLWDDGVIDPADTRTVVGLALSVVGQAPLEPVSYGVFRM

Entity 2 Entity 2 polymer

Description description	biotin carboxylase
Molecular weight formula_weight	70144.7 kDa
EC 编号 ec_number	6.3.4.14
Source method src_method	nat
Copy count entity_count	6

Polymer Polymer

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

MMMSSQTFDTVLVANRGEIAVRVIRTLRAMGIRSVAVFSEADAGARHVTEADVAVCIGPAAARHSYLDIDAVVGAARRTDAQAVHPGYGFLSENAEFASALATAGIVFIGPPASAIATMGDKIAAKAAVSAFGVPVVPGISRPGLADDDLIAGAAEVGYPVLVKPSAGGGGKGMRVVEAAADLPAALVSARREAGAAFGDDTLFLERFVQRPRHIEVQVLADGHGNVIHLGERECSLQRRHQKVIEEAPSPLLDEATRARIGAAACATARSVDYTGAGTVEFIVSADRPDEFFFMEMNTRLQVEHPVTELVTGIDLVEQQIRIAAGEPLAIGQDDITLTGHAVEARVYAEDPAAGFLPTGGDVLGLREPTGRGVRVDSGLAAGTVVGSDYDPMLSKIIAHGSDRASALQILDRALADTAVLGVTTNIEFLRFLLADDDVAAGRLDTGLLDRRAPDFAPATVGDEQLIAAAAYLWARQWSAAGGDLWRVPSGWRVGEWAPATFRLHAGDRTDHVYITGNPERASAAVEHGDTHTVSADFTPGSDTFAVTLDGLRTDYRVAVTDSQIWLSGGGRTWSVQKVREEPVRPDDAHSGDAELVSPMPGSVVAVGVPDGSDVTAGTVVVTVEAMKMEHALTAPVDGVAKILVAVGDQVKVGQPLARITAHTQENES

Entity 3 Entity 3 non-polymer

Description description	BIOTIN
Molecular weight formula_weight	244.3 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	2.000 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	2.00 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	30234

Structure of the 3-methylcrotonyl-coenzyme A carboxylase from Mycobacterium smegmatis

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

Carboxyl transferase domain protein

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

9yx0__assembly_1__model_1

9yx0__assembly_1__model_1 | I(q)

9yx0__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

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)

Structure of the 3-methylcrotonyl-coenzyme A carboxylase from Mycobacterium smegmatis

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

Carboxyl transferase domain protein

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

9yx0__assembly_1__model_1

9yx0__assembly_1__model_1 | I(q)

9yx0__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

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)