SAXSdb — 8xl2

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

Acetyl-CoA carboxylase 1

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–2346 Chain B； UniProt 1–2346 Chain C； UniProt 1–2346 Chain D； UniProt 1–2346	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

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 8XL2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2YL2 Crystal structure of human acetyl-CoA carboxylase 1, biotin carboxylase (BC) domain Deposited 2011-05-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 78–617（540 aa） Fragment：BIOTIN CARBOXYLASE (BC) DOMAIN, RESIDUES 78-617	Not recorded	No recorded non-water small molecule	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
2YL2 Crystal structure of human acetyl-CoA carboxylase 1, biotin carboxylase (BC) domain Deposited 2011-05-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 78–617（540 aa） Fragment：BIOTIN CARBOXYLASE (BC) DOMAIN, RESIDUES 78-617	Not recorded	No recorded non-water small molecule	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
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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 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 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 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

9 other PDB entries and 19 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 1–2346； UniProt 1–2346 Author chain B； PDBConstruct 1–2346； UniProt 1–2346 Author chain C； PDBConstruct 1–2346； UniProt 1–2346 Author chain D； PDBConstruct 1–2346； UniProt 1–2346

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	8xl2
Deposition date deposition_date	2023-12-25
最后修订 last_revision	2024-10-23
Structure title title	Human acetyl-CoA carboxylase 1 filament in complex with acetyl-CoA (ACC1-inact)
Keywords keywords	Biotin-dependent carboxylase, LIGASE; LIGASE
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	91.64 Å
Radius of gyration Rg (electron density) rg_electron	94.21 Å
Forward intensity I(0) i0	4359050000.00
Molecular weight molecular_weight	562460.0 kDa
Excluded volume excluded_volume	705500 Å³
Envelope volume envelope_volume	1199600 Å³
Hydration-shell volume shell_volume	121580 Å³
Envelope diameter envelope_diameter	331.0 Å
Shell Rg shell_rg	65.52 Å
Envelope Rg envelope_rg	93.74 Å
Shape Rg shape_rg	94.21 Å
Total Rg total_rg	93.80 Å
Total atoms total_atoms	39556
Residues n_residues	4901
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	258.6 Å
Rg (real space) rg_real	85.84 Å
Rg uncertainty (real space) rg_real_error	1.39 Å
I(0) (real space) i0_real	4.1800e+09
I(0) uncertainty (real space) i0_real_error	8.8740e+07
Rg (reciprocal space) rg_reciprocal	83.67 Å
I(0) (reciprocal space) i0_reciprocal	4255000000.0000
Solution quality estimate total_estimate	0.8714
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	60.8 Å
Skewness Skewness skewness	0.471
Kurtosis Kurtosis kurtosis	-0.724
Angular range angular_range	— – 0.0850 Å⁻¹
Current regularization parameter α current_alpha	0.7229
Highest regularization parameter α highest_alpha	162700000.0000
Real-space data points n_real_points	18
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.001; Oscil: 0.822; Stabil: 0.974; Sysdev: 1.000; Positv: 1.000; Valcen: 0.948; Smooth: 0.006

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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	265869.4 kDa
EC 编号 ec_number	6.4.1.2
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,D,C
Atom count atom_count	39556

MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVGSDTLSDLGISSLQDGLALHIRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEKVLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMYGVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVSLRNSVSNFLHSLERGQVLPAHTLLNTVDVELIYEGVKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDGSSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVLAKMQLDNPSKVQQAELHTGSLPRIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSKVKDWVERLMKTLRDPSLPLLELQDIMTSVSGRIPPNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFSSNLNHYGMTHVASVSDVLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSPPQSPTFPEAGHTSLYDEDKVPRDEPIHILNVAIKTDCDIEDDRLAAMFREFTQQNKATLVDHGIRRLTFLVAQKDFRKQVNYEVDRRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFEYLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTPTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQAYGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQAFLPSPPLPSDMLTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMTFKSPEYPEGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGARIGLAEEIRHMFHVAWVDPEDPYKGYRYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGIGPENLRGSGMIAGESSLAYNEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGREVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDPIDRIIEFVPTKTPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECCQPVLVYIPPQAELRGGSWVVIDSSINPRHMEMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRRVDPVYIHLAERLGTPELSTAERKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRTFFYWRLRRLLLEDLVKKKIHNANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLAEWLEKQLTEEDGVHSVIEENIKCISRDYVLKQIRSLVQANPEVAMDSIIHMTQHISPTQRAEVIRILSTMDSPST

Entity 2 Entity 2 non-polymer

Description description	ACETYL COENZYME *A
Molecular weight formula_weight	809.6 kDa
Source method src_method	syn
Copy count entity_count	3

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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	triclinic

Resolution resolution	2.73 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	155033

fit	/app/data/saxs_computation/xl/8xl2/8xl2.fit
pddf	/app/data/pr_computation/xl/8xl2/8xl2.pr.out
profile	/app/data/saxs_computation/xl/8xl2/8xl2.dat

Human acetyl-CoA carboxylase 1 filament in complex with acetyl-CoA (ACC1-inact)

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)