8uxz

E. coli acetyl-CoA carboxylase, wide stacked local reconstruction, 3.20 Angstrom

Method: ELECTRON MICROSCOPY
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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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 9 Biotin carboxyl carrier protein of acetyl-CoA carboxylase × 2 (P0ABD8) Biotin carboxylase × 2 (P24182) Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta × 3 (P0A9Q5) BIOTIN × 2 ADENOSINE-5'-DIPHOSPHATE × 2 MAGNESIUM ION × 2 ZINC ION × 2 ACETYL COENZYME *A × 2 Consistent with protein count

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 9 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha × 2 (P0ABD5) Biotin carboxylase × 2 (P24182) Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta × 3 (P0A9Q5) BIOTIN × 2 ADENOSINE-5'-DIPHOSPHATE × 2 MAGNESIUM ION × 2 ZINC ION × 2 ACETYL COENZYME *A × 2 Consistent with protein count

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 9 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) BIOTIN × 2 ADENOSINE-5'-DIPHOSPHATE × 2 MAGNESIUM ION × 2 ZINC ION × 2 ACETYL COENZYME *A × 2 Consistent with protein count

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 9 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha × 2 (P0ABD5) Biotin carboxyl carrier protein of acetyl-CoA carboxylase × 2 (P0ABD8) Biotin carboxylase × 2 (P24182) BIOTIN × 2 ADENOSINE-5'-DIPHOSPHATE × 2 MAGNESIUM ION × 2 ZINC ION × 2 ACETYL COENZYME *A × 2 Consistent with protein count

Other States of the Same Protein in the Database

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id8uxz
Deposition date deposition_date2023-11-11
Structure title titleE. coli acetyl-CoA carboxylase, wide stacked local reconstruction, 3.20 Angstrom
Keywords keywordscomplex, enzyme, biosynthesis of fatty acids, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method methodELECTRON 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.

8uxz__assembly_1__model_1

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

Download this curve (.dat)

8uxz__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8uxz__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)53.61 Å
Rg (electron density)54.05 Å
Total Rg54.03 Å
Atom count17474
Residues2246
Excluded volume312000 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8uxz__assembly_1__model_1 nonameric (9) 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 (9)

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7. Citations (1)