SAXSdb — 30hu

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

Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit

OrganismNot specified

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain A3a； UniProt 1–598 Chain A3b； UniProt 1–598 Chain A3c； UniProt 1–598 Chain A3d； UniProt 1–598	Not recorded	Acetyl-/propionyl-coenzyme A carboxylase AccE5 × 1 （A0QTE6） ADENOSINE-5'-TRIPHOSPHATE × 1 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL × 1	ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions	Resolution 3.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 30HU	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9T97 cryo-EM structure of AccA3/AccD4/AccD5/AccE5 complex from Mycobacterium smegmatis Deposited 2025-11-14	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: 15-meric	Chain A3a 1–598（598 aa） Chain A3b 1–598（598 aa） Chain A3c 1–598（598 aa） Chain A3d 1–598（598 aa） Chain A3f 1–598（598 aa） Chain A3g 1–598（598 aa） Chain A3i 1–598（598 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 2.35 Å
9TDM Cryo-EM structure of AccA3/AccD4/AccD5/AccE5 in complex with Propionyl-CoA Deposited 2025-11-24	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric	Chain A3a 1–598（598 aa） Chain A3b 1–598（598 aa） Chain A3c 1–598（598 aa） Chain A3d 1–598（598 aa） Chain A3e 1–598（598 aa） Chain A3f 1–598（598 aa） Chain A3g 1–598（598 aa） Chain A3h 1–598（598 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 2.40 Å
9YX1 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis Deposited 2025-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric	Chain A 1–598（598 aa） Chain B 1–598（598 aa） Chain C 1–598（598 aa） Chain D 1–598（598 aa） Chain I 1–598（598 aa） Chain J 1–598（598 aa） Chain K 1–598（598 aa） Chain L 1–598（598 aa） Chain Q 1–598（598 aa） Chain R 1–598（598 aa） Chain S 1–598（598 aa） Chain T 1–598（598 aa）	Not recorded	BTN BIOTIN × 6 BCT BICARBONATE ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9YX2 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, and propionyl-CoA Deposited 2025-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric	Chain A 1–598（598 aa） Chain B 1–598（598 aa） Chain C 1–598（598 aa） Chain D 1–598（598 aa） Chain I 1–598（598 aa） Chain J 1–598（598 aa） Chain K 1–598（598 aa） Chain L 1–598（598 aa） Chain Q 1–598（598 aa） Chain R 1–598（598 aa） Chain S 1–598（598 aa） Chain T 1–598（598 aa）	Not recorded	BTN BIOTIN × 6 BCT BICARBONATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 MG MAGNESIUM ION × 8 1VU propionyl Coenzyme A × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
9YX4 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, arachidoyl-CoA, and propionyl-CoA Deposited 2025-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric	Chain A 1–598（598 aa） Chain B 1–598（598 aa） Chain C 1–598（598 aa） Chain D 1–598（598 aa） Chain I 1–598（598 aa） Chain J 1–598（598 aa） Chain K 1–598（598 aa） Chain L 1–598（598 aa） Chain Q 1–598（598 aa） Chain R 1–598（598 aa） Chain S 1–598（598 aa） Chain T 1–598（598 aa）	Not recorded	BTN BIOTIN × 6 BCT BICARBONATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 MG MAGNESIUM ION × 8 A1CZD S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) × 2 1VU propionyl Coenzyme A × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
9YX5 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with MSMEG_0435-MSMEG_0436 bound Deposited 2025-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 26 PDB declaration: 26-meric	Chain A 1–598（598 aa） Chain B 1–598（598 aa） Chain C 1–598（598 aa） Chain D 1–598（598 aa） Chain I 1–598（598 aa） Chain J 1–598（598 aa） Chain K 1–598（598 aa） Chain L 1–598（598 aa） Chain Q 1–598（598 aa） Chain R 1–598（598 aa） Chain S 1–598（598 aa） Chain T 1–598（598 aa） Chain U 1–598（598 aa） Chain X 1–598（598 aa）	Not recorded	A1CZD S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) × 2 1VU propionyl Coenzyme A × 4 BTN BIOTIN × 5 BCT BICARBONATE ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0QTE1_MYCS2
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A3a； PDBConstruct 1–598； UniProt 1–598 Author chain A3b； PDBConstruct 1–598； UniProt 1–598 Author chain A3c； PDBConstruct 1–598； UniProt 1–598 Author chain A3d； PDBConstruct 1–598； UniProt 1–598

Acetyl-/propionyl-coenzyme A carboxylase AccE5

OrganismNot specified

UniProt A0QTE6

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain E5a； UniProt 1–94	Not recorded	Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit × 4 （A0QTE1） ADENOSINE-5'-TRIPHOSPHATE × 1 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL × 1	ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions	Resolution 3.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 30HU	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9T97 cryo-EM structure of AccA3/AccD4/AccD5/AccE5 complex from Mycobacterium smegmatis Deposited 2025-11-14	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: 15-meric	Chain E5a 1–94（94 aa） Chain E5b 1–94（94 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 2.35 Å
9TDM Cryo-EM structure of AccA3/AccD4/AccD5/AccE5 in complex with Propionyl-CoA Deposited 2025-11-24	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric	Chain E5a 1–94（94 aa） Chain E5b 1–94（94 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 2.40 Å
9YX1 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis Deposited 2025-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric	Chain E 1–94（94 aa） Chain P 1–94（94 aa）	Not recorded	BTN BIOTIN × 6 BCT BICARBONATE ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9YX2 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, and propionyl-CoA Deposited 2025-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric	Chain E 1–94（94 aa） Chain P 1–94（94 aa）	Not recorded	BTN BIOTIN × 6 BCT BICARBONATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 MG MAGNESIUM ION × 8 1VU propionyl Coenzyme A × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
9YX4 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, arachidoyl-CoA, and propionyl-CoA Deposited 2025-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric	Chain E 1–94（94 aa） Chain P 1–94（94 aa）	Not recorded	BTN BIOTIN × 6 BCT BICARBONATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 8 MG MAGNESIUM ION × 8 A1CZD S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) × 2 1VU propionyl Coenzyme A × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
9YX5 Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with MSMEG_0435-MSMEG_0436 bound Deposited 2025-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 26 PDB declaration: 26-meric	Chain E 1–94（94 aa） Chain P 1–94（94 aa）	Not recorded	A1CZD S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) × 2 1VU propionyl Coenzyme A × 4 BTN BIOTIN × 5 BCT BICARBONATE ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0QTE6_MYCS2
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E5a； PDBConstruct 1–94； UniProt 1–94

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	30hu
Deposition date deposition_date	2026-04-27
Structure title title	cryo-EM structure of AccA3-AccE5 complex in the presence of Arachidyl-CoA
Keywords keywords	Bio-dependent acyl-CoA carboxylase, AccA3-AccE5 complex, TRANSFERASE; TRANSFERASE
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	50.95 Å
Radius of gyration Rg (electron density) rg_electron	50.91 Å
Forward intensity I(0) i0	712231000.00
Molecular weight molecular_weight	219720.0 kDa
Excluded volume excluded_volume	274220 Å³
Envelope volume envelope_volume	406310 Å³
Hydration-shell volume shell_volume	66605 Å³
Envelope diameter envelope_diameter	157.4 Å
Shell Rg shell_rg	54.12 Å
Envelope Rg envelope_rg	49.44 Å
Shape Rg shape_rg	50.91 Å
Total Rg total_rg	50.99 Å
Total atoms total_atoms	15502
Residues n_residues	2045
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	149.6 Å
Rg (real space) rg_real	51.00 Å
Rg uncertainty (real space) rg_real_error	1.20 Å
I(0) (real space) i0_real	7.1220e+08
I(0) uncertainty (real space) i0_real_error	1.4470e+07
Rg (reciprocal space) rg_reciprocal	50.88 Å
I(0) (reciprocal space) i0_reciprocal	712100000.0000
Solution quality estimate total_estimate	0.8393
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	38.6 Å
Skewness Skewness skewness	0.229
Kurtosis Kurtosis kurtosis	-0.797
Angular range angular_range	— – 0.1550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	120200000.0000
Real-space data points n_real_points	32
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.981; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.001

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit
Molecular weight formula_weight	63215.2 kDa
EC 编号 ec_number	6.3.4.14
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A3a,A3b,A3c,A3d
Atom count atom_count	15502

MANHASSKISKVLVANRGEIAVRVIRAAKDAGLASVAVYAEPDADAPHVRLADEAFALGGQTSAESYLVFEKILDAAEKSGANAIHPGYGFLSENADFAQAVIDAGLIWIGPSPQSIRDLGDKVTARHIAARAKAPLVPGTPDPVKDADEVVAFAKEHGVPVAIKAAFGGGGRGMKVARTLEEIPELFESATREAIAAFGRGECFVERYLDKPRHVEAQVIADQHGNVVVAGTRDCSLQRRFQKLVEEAPAPFLTDAQRKEIHESAKRICKEAGYYGAGTVEYLVGQDGLISFLEVNTRLQVEHPVTEETSGIDLVRQQFKIANGEPLDITEDPTPRGHSFEFRINGEDAGRGFLPAPGPVTKFVAPTGPGVRMDSGVETGSVIGGQFDSMLAKLIVTGATREEALERSRRALAEFTVEGLATVIPFHRAVVSDPAFIGDGEKFDVHTRWIETEWNNTVEPFTGGDPIEEEDTVPRQTVVVEVGGRRLEVSLPGDLAIGGGGGAAAPGVVRKKPKPRKRGGGGAKAASGDAVTAPMQGTVVKVAVEEGQEVSAGDLVVVLEAMKMENPVTAHKDGTITGLAVEAGAAITQGTVIAEIK

Entity 2 Entity 2 polymer

Description description	Acetyl-/propionyl-coenzyme A carboxylase AccE5
Molecular weight formula_weight	10357.7 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E5a

MSGANDSTTVSGEVQADVTDEAKADHEAHIKVLRGEPTPEEMAALMAVLASAGGGPAEPVKKERNMWGHPVDKLRYSVFSWQRVTLLERTHMRR

Entity 3 Entity 3 non-polymer

Description description	ADENOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	507.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 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	1

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8. Citations (1)

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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	3.500 Å
Low-resolution limit resolution_low	375.200 Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	3.50 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	76111

fit	/app/data/saxs_computation/0h/30hu/30hu.fit
pddf	/app/data/pr_computation/0h/30hu/30hu.pr.out
profile	/app/data/saxs_computation/0h/30hu/30hu.dat

cryo-EM structure of AccA3-AccE5 complex in the presence of Arachidyl-CoA

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

Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit

State in the Current Structure

Other States of the Same Protein in the Database

Acetyl-/propionyl-coenzyme A carboxylase AccE5

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)