SAXSdb — 2yl2

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

ACETYL-COA CARBOXYLASE 1

HOMO SAPIENS

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 78–617	Fragment：BIOTIN CARBOXYLASE (BC) DOMAIN, RESIDUES 78-617	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：20% PEG 3350, 200 MM NA(MALONATE) PH 7.0	Resolution 2.30 Å R-free 0.241
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 78–617	Fragment：BIOTIN CARBOXYLASE (BC) DOMAIN, RESIDUES 78-617	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：20% PEG 3350, 200 MM NA(MALONATE) PH 7.0	Resolution 2.30 Å R-free 0.241

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 2YL2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 1258–1270（13 aa） Fragment：residues 1258-1270	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 1258–1270（13 aa） Fragment：residues 1258-1270	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain J 1258–1270（13 aa） Fragment：residues 1258-1270	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain K 1258–1270（13 aa） Fragment：residues 1258-1270	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 1258–1270（13 aa） Fragment：residues 1258-1270	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain M 1258–1270（13 aa） Fragment：residues 1258-1270	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain N 1258–1270（13 aa） Fragment：residues 1258-1270	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
3COJ Crystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1 Deposited 2008-03-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 8 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain O 1258–1270（13 aa） Fragment：residues 1258-1270	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；294 K；100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 3.21 Å R-free 0.307
4ASI Crystal structure of human ACACA C-terminal domain Deposited 2012-05-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1493–2260（768 aa） Fragment：C-TERMINAL DOMAIN, RESIDUES 1493-2260 Chain C 1493–2260（768 aa） Fragment：C-TERMINAL DOMAIN, RESIDUES 1493-2260	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions 0.05M NA MALONATE; 19% (W/V) PEG3350	Resolution 2.80 Å R-free 0.236
4ASI Crystal structure of human ACACA C-terminal domain Deposited 2012-05-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1493–2260（768 aa） Fragment：C-TERMINAL DOMAIN, RESIDUES 1493-2260 Chain D 1493–2260（768 aa） Fragment：C-TERMINAL DOMAIN, RESIDUES 1493-2260	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions 0.05M NA MALONATE; 19% (W/V) PEG3350	Resolution 2.80 Å R-free 0.236
4ASI Crystal structure of human ACACA C-terminal domain Deposited 2012-05-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 1493–2260（768 aa） Fragment：C-TERMINAL DOMAIN, RESIDUES 1493-2260 Chain F 1493–2260（768 aa） Fragment：C-TERMINAL DOMAIN, RESIDUES 1493-2260	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions 0.05M NA MALONATE; 19% (W/V) PEG3350	Resolution 2.80 Å R-free 0.236
6G2D Citrate-induced acetyl-CoA carboxylase (ACC-Cit) filament at 5.4 A resolution Deposited 2018-03-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 1–2346（2346 aa） Chain C 1–2346（2346 aa） Chain D 1–2346（2346 aa） Chain F 1–2346（2346 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.40 Å
6G2H Filament of acetyl-CoA carboxylase and BRCT domains of BRCA1 (ACC-BRCT) core at 4.6 A resolution Deposited 2018-03-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–2346（2346 aa） Chain B 1–2346（2346 aa） Chain C 1–2346（2346 aa） Chain D 1–2346（2346 aa） Chain E 1–2346（2346 aa） Chain F 1–2346（2346 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.60 Å
6G2I Filament of acetyl-CoA carboxylase and BRCT domains of BRCA1 (ACC-BRCT) at 5.9 A resolution Deposited 2018-03-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain A 1–2346（2346 aa） Chain B 1–2346（2346 aa） Chain C 1–2346（2346 aa） Chain D 1–2346（2346 aa） Chain E 1–2346（2346 aa） Chain F 1–2346（2346 aa） Chain G 1–2346（2346 aa） Chain J 1–2346（2346 aa） Chain Q 1–2346（2346 aa） Chain R 1–2346（2346 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.90 Å
8XKZ Core region of the citrate-induced human acetyl-CoA carboxylase 1 filament (ACC1-citrate) Deposited 2023-12-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 98–2337（2240 aa） Chain D 98–2337（2240 aa）	Not recorded	BTN BIOTIN × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.55 Å
8XL0 Citrate-induced filament of human acetyl-coenzyme A carboxylase 1 (ACC1-citrate) Deposited 2023-12-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–2346（2346 aa） Chain B 1–2346（2346 aa） Chain C 1–2346（2346 aa） Chain D 1–2346（2346 aa） Chain E 1–2346（2346 aa） Chain F 1–2346（2346 aa）	Not recorded	BTN BIOTIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.14 Å
8XL1 Core region of the human acetyl-CoA carboxylase 1 filament in complex with acetyl-CoA (ACC1-inact) Deposited 2023-12-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–2346（2346 aa） Chain B 1–2346（2346 aa）	Not recorded	ACO ACETYL COENZYME *A × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.57 Å
8XL2 Human acetyl-CoA carboxylase 1 filament in complex with acetyl-CoA (ACC1-inact) Deposited 2023-12-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–2346（2346 aa） Chain B 1–2346（2346 aa） Chain C 1–2346（2346 aa） Chain D 1–2346（2346 aa）	Not recorded	ACO ACETYL COENZYME *A × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å

9 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACACA_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–540； UniProt 78–617 Author chain B； PDBConstruct 1–540； UniProt 78–617

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	2yl2
Deposition date deposition_date	2011-05-31
Structure title title	Crystal structure of human acetyl-CoA carboxylase 1, biotin carboxylase (BC) domain
Keywords keywords	LIGASE; LIGASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	33.11 Å
Radius of gyration Rg (electron density) rg_electron	32.40 Å
Forward intensity I(0) i0	169922000.00
Molecular weight molecular_weight	104830.0 kDa
Excluded volume excluded_volume	131410 Å³
Envelope volume envelope_volume	168080 Å³
Hydration-shell volume shell_volume	43199 Å³
Envelope diameter envelope_diameter	106.7 Å
Shell Rg shell_rg	39.49 Å
Envelope Rg envelope_rg	31.59 Å
Shape Rg shape_rg	32.40 Å
Total Rg total_rg	33.00 Å
Total atoms total_atoms	7384
Residues n_residues	968
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	105.7 Å
Rg (real space) rg_real	33.08 Å
Rg uncertainty (real space) rg_real_error	0.73 Å
I(0) (real space) i0_real	1.6990e+08
I(0) uncertainty (real space) i0_real_error	2.6800e+06
Rg (reciprocal space) rg_reciprocal	33.10 Å
I(0) (reciprocal space) i0_reciprocal	169900000.0000
Solution quality estimate total_estimate	0.8959
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	37.4 Å
Skewness Skewness skewness	0.295
Kurtosis Kurtosis kurtosis	-0.543
Angular range angular_range	— – 0.2400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	35430000.0000
Real-space data points n_real_points	49
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.888

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	ACETYL-COA CARBOXYLASE 1
Molecular weight formula_weight	60241.5 kDa
EC 编号 ec_number	6.4.1.2, 6.3.4.14
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	7627

SMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEKVLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMYGVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLETESFQMNRIDTGWLDRLI

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	213

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7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id	2yl2A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2yl2A02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1770 — PreATP-grasp fold
Homologous superfamily homologous superfamily	10 — PreATP-grasp domain

Domain ID domain_id	2yl2A03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, A domain

Domain ID domain_id	2yl2A04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, B domain

Domain ID domain_id	2yl2B01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2yl2B02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1770 — PreATP-grasp fold
Homologous superfamily homologous superfamily	10 — PreATP-grasp domain

Domain ID domain_id	2yl2B03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, A domain

Domain ID domain_id	2yl2B04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, B domain

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8. Citations (1)

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Unit-cell length a length_a	60.670 Å
Unit-cell length b length_b	60.870 Å
Unit-cell length c length_c	70.370 Å
Unit-cell angle α angle_alpha	92.04 °
Unit-cell angle β angle_beta	98.00 °
Unit-cell angle γ angle_gamma	92.20 °
Molecules per unit cell Z z_pdb	2

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

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	33.670 Å
R factor r_factor	0.2076
R_work r_work	0.2058
R_free r_free	0.2407

fit	/app/data/saxs_computation/yl/2yl2/2yl2.fit
pddf	/app/data/pr_computation/yl/2yl2/2yl2.pr.out
profile	/app/data/saxs_computation/yl/2yl2/2yl2.dat

Crystal structure of human acetyl-CoA carboxylase 1, biotin carboxylase (BC) domain

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

ACETYL-COA CARBOXYLASE 1

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

Diffraction experiment Diffraction