8uz2

E. coli acetyl-CoA carboxylase, narrow helical local reconstruction, 3.18 Angstrom

Method: ELECTRON MICROSCOPY Dmax: 191.3 Å Quality: GOOD

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

Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha

Escherichia coli

UniProt P0ABD5

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 4–319 Chain E; UniProt 4–319 Not recorded Biotin carboxyl carrier protein of acetyl-CoA carboxylase × 2 (P0ABD8) Biotin carboxylase × 2 (P24182) Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta × 3 (P0A9Q5) BTN BIOTIN × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 ACO ACETYL COENZYME *A × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;2.5 mg/ml ACC complex in 50 mM HEPES pH 7.5, 100 mM bicarbonate, 7.5 mM ATP, 20 mM MgCl2 and 1 mM acetyl-CoA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACCA_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–316; UniProt 4–319 Author chain E; PDBConstruct 1–316; UniProt 4–319

Biotin carboxyl carrier protein of acetyl-CoA carboxylase

Escherichia coli

UniProt P0ABD8

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 80–156 Chain F; UniProt 80–156 Not recorded Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha × 2 (P0ABD5) Biotin carboxylase × 2 (P24182) Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta × 3 (P0A9Q5) BTN BIOTIN × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 ACO ACETYL COENZYME *A × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;2.5 mg/ml ACC complex in 50 mM HEPES pH 7.5, 100 mM bicarbonate, 7.5 mM ATP, 20 mM MgCl2 and 1 mM acetyl-CoA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BCCP_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–77; UniProt 80–156 Author chain F; PDBConstruct 1–77; UniProt 80–156

Biotin carboxylase

Escherichia coli

UniProt P24182

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain C; UniProt 1–446 Chain G; UniProt 1–446 Not recorded Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha × 2 (P0ABD5) Biotin carboxyl carrier protein of acetyl-CoA carboxylase × 2 (P0ABD8) Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta × 3 (P0A9Q5) BTN BIOTIN × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 ACO ACETYL COENZYME *A × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;2.5 mg/ml ACC complex in 50 mM HEPES pH 7.5, 100 mM bicarbonate, 7.5 mM ATP, 20 mM MgCl2 and 1 mM acetyl-CoA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

29 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACCC_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–446; UniProt 1–446 Author chain G; PDBConstruct 1–446; UniProt 1–446

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Escherichia coli

UniProt P0A9Q5

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain D; UniProt 2–285 Chain H; UniProt 2–285 Chain I; UniProt 2–285 Not recorded Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha × 2 (P0ABD5) Biotin carboxyl carrier protein of acetyl-CoA carboxylase × 2 (P0ABD8) Biotin carboxylase × 2 (P24182) BTN BIOTIN × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 ACO ACETYL COENZYME *A × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;2.5 mg/ml ACC complex in 50 mM HEPES pH 7.5, 100 mM bicarbonate, 7.5 mM ATP, 20 mM MgCl2 and 1 mM acetyl-CoA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACCD_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–284; UniProt 2–285 Author chain H; PDBConstruct 1–284; UniProt 2–285 Author chain I; PDBConstruct 1–284; UniProt 2–285

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.

SAXS scattering curve SAXS Profile

SAXS profile for 8uz2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8uz2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8uz2
Deposition date deposition_date2023-11-14
最后修订 last_revision2024-11-20
Structure title titleE. coli acetyl-CoA carboxylase, narrow helical local reconstruction, 3.18 Angstrom
Keywords keywordscomplex, enzyme, biosynthesis of fatty acids, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.31
Radius of gyration Rg (electron density) rg_electron53.70
Forward intensity I(0) i0919420000.00
Molecular weight molecular_weight249780.0 kDa
Excluded volume excluded_volume312000 ų
Envelope volume envelope_volume439500 ų
Hydration-shell volume shell_volume70691 ų
Envelope diameter envelope_diameter188.5
Shell Rg shell_rg53.30
Envelope Rg envelope_rg53.00
Shape Rg shape_rg53.70
Total Rg total_rg53.70
Total atoms total_atoms17474
Residues n_residues2246
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax191.3
Rg (real space) rg_real53.70
Rg uncertainty (real space) rg_real_error2.32
I(0) (real space) i0_real9.1940e+08
I(0) uncertainty (real space) i0_real_error1.8430e+07
Rg (reciprocal space) rg_reciprocal52.97
I(0) (reciprocal space) i0_reciprocal918500000.0000
Solution quality estimate total_estimate0.8224
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.6
Skewness Skewness skewness0.480
Kurtosis Kurtosis kurtosis-0.521
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha79670000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.673; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.853; Smooth: 0.814

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)