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1a6x

STRUCTURE OF THE APO-BIOTIN CARBOXYL CARRIER PROTEIN (APO-BCCP87) OF ESCHERICHIA COLI ACETYL-COA CARBOXYLASE, NMR, 49 STRUCTURES

Method: SOLUTION NMR Dmax: 36.6 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

APO-BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE

Escherichia coli BL21(DE3)

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 70–156 Fragment：CARBOXYL-TERMINAL FRAGMENT, RESIDUES 70 - 156 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7.5；298 K NMR sample composition：PHOSPHATE BUFFER Resolution not provided

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 1A6X Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BDO STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING Deposited 1995-11-21 Different construct 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 77–156（80 aa） Fragment：BIOTINYL DOMAIN, RESIDUES 77 - 156
Not recorded BTN BIOTIN × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å
2BDO SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY Deposited 1999-03-03 Different construct Different ligand/ion Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 77–156（80 aa） Fragment：BIOTINYL DOMAIN, RESIDUES 77 - 156
Not recorded BTN BIOTIN × 1 SOLUTION NMR
NMR measurement conditions pH 6.8；303 K；Ionic strength (raw mmCIF value) 20mM SODIUM PHOSPHATE；Pressure 1
Resolution not provided
3BDO SOLUTION STRUCTURE OF APO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY Deposited 1999-03-08 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 75–156（82 aa） Fragment：BIOTINYL DOMAIN, RESIDUES 77 - 156
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；303 K；Ionic strength (raw mmCIF value) 20mM SODIUM PHOSPHATE；Pressure 1
NMR sample composition 90% WATER/10% D2O
Resolution not provided
4HR7 Crystal Structure of Biotin Carboxyl Carrier Protein-Biotin Carboxylase Complex from E.coli Deposited 2012-10-26 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 × 8 PDB declaration: octameric
Chain B 1–156（156 aa）
Chain D 1–156（156 aa）
Chain G 1–156（156 aa）
Chain I 1–156（156 aa）
Not recorded SO4 SULFATE ION × 12 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；295.15 K；0.2 M ammonium sulfate, 0.1 M Bis-Tris, pH 6.5, 25% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 295.15K
Resolution 2.50 Å R-free 0.229
8UXZ E. coli acetyl-CoA carboxylase, wide stacked local reconstruction, 3.20 Angstrom Deposited 2023-11-11 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 × 9 PDB declaration: nonameric
Chain B 80–156（77 aa）
Chain F 80–156（77 aa）
Not recorded 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 3.20 Å
8UZ2 E. coli acetyl-CoA carboxylase, narrow helical local reconstruction, 3.18 Angstrom Deposited 2023-11-14 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 × 9 PDB declaration: nonameric
Chain B 80–156（77 aa）
Chain F 80–156（77 aa）
Not recorded 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
9E4N E. coli acetyl-CoA carboxylase, narrow helical tube, 4.04 Angstrom Deposited 2024-10-25 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 152 PDB declaration: 152-meric
Chain B 80–156（77 aa）
Not recorded BTN BIOTIN × 38 ADP ADENOSINE-5'-DIPHOSPHATE × 38 MG MAGNESIUM ION × 38 ZN ZINC ION × 38 ACO ACETYL COENZYME *A × 38 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 4.04 Å
9E4O E. coli acetyl-CoA carboxylase, wide stacked tube, 3.98 Angstrom Deposited 2024-10-25 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 160 PDB declaration: 160-meric
Chain B 80–156（77 aa）
Not recorded BTN BIOTIN × 40 ADP ADENOSINE-5'-DIPHOSPHATE × 40 MG MAGNESIUM ION × 40 ZN ZINC ION × 40 ACO ACETYL COENZYME *A × 40 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 3.98 Å

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 1
Chains and sequence ranges Author chain A； PDBConstruct 1–87； UniProt 70–156

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 1a6x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a6x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a6x
Deposition date deposition_date1998-03-04
Structure title titleSTRUCTURE OF THE APO-BIOTIN CARBOXYL CARRIER PROTEIN (APO-BCCP87) OF ESCHERICHIA COLI ACETYL-COA CARBOXYLASE, NMR, 49 STRUCTURES
Keywords keywordsACETYL-COA CARBOXYLASE, BIOTIN CARBOXYL CARRIER PROTEIN, BACKBONE DYNAMICS, CARRIER PROTEIN; CARRIER PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier13.65 Å
Radius of gyration Rg (electron density) rg_electron13.54 Å
Forward intensity I(0) i02794900000.00
Molecular weight molecular_weight456230.0 kDa
Excluded volume excluded_volume573480 ų
Envelope volume envelope_volume44027 ų
Hydration-shell volume shell_volume18155 ų
Envelope diameter envelope_diameter67.6 Å
Shell Rg shell_rg27.51 Å
Envelope Rg envelope_rg22.35 Å
Shape Rg shape_rg13.46 Å
Total Rg total_rg14.03 Å
Total atoms total_atoms59094
Residues n_residues4263
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax36.6 Å
Rg (real space) rg_real12.80 Å
Rg uncertainty (real space) rg_real_error0.05 Å
I(0) (real space) i0_real2.6630e+09
I(0) uncertainty (real space) i0_real_error2.2450e+07
Rg (reciprocal space) rg_reciprocal13.75 Å
I(0) (reciprocal space) i0_reciprocal2795000000.0000
Solution quality estimate total_estimate0.6808
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary15.7 Å
Skewness Skewness skewness0.199
Kurtosis Kurtosis kurtosis-0.300
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha4.2430
Highest regularization parameter α highest_alpha116900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.980; Stabil: 0.973; Sysdev: 0.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1a6xa_
Class classb — All beta proteins
Fold Fold foldb.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamilyb.84.1 — Single hybrid motif
Family Family familyb.84.1.1 — Biotinyl/lipoyl-carrier proteins and domains

CATH v4.4 (1 domains)

Domain ID domain_id1a6xA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain
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8. Citations (1)

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9. Files and Curves (10)