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1aca

THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN ACYL-COENZYME A BINDING PROTEIN AND PALMITOYL-COENZYME A

Method: SOLUTION NMR Dmax: 41.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ACYL-COENZYME A BINDING PROTEIN

Bos taurus

UniProt P07107

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 1–86 Not recorded COA COENZYME A × 1 PLM PALMITIC ACID × 1 SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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 1ACA Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1HB6 Structure of bovine Acyl-CoA binding protein in orthorhombic crystal form Deposited 2001-04-12 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 1–86（86 aa）
Not recorded CD CADMIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；15% PEG8000, 5MMCDCL2, 10MM HEPES PH7.5, pH 7.50
Resolution 2.00 Å R-free 0.226
1HB8 Structure of bovine Acyl-CoA binding protein in tetragonal crystal form Deposited 2001-04-12 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 1–86（86 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；25% PEG5000 MME, 40MM NI(SO4)2, 40MM HEPES PH7.5, pH 7.50
Resolution 2.00 Å R-free 0.255
1HB8 Structure of bovine Acyl-CoA binding protein in tetragonal crystal form Deposited 2001-04-12 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 1–86（86 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；25% PEG5000 MME, 40MM NI(SO4)2, 40MM HEPES PH7.5, pH 7.50
Resolution 2.00 Å R-free 0.255
1HB8 Structure of bovine Acyl-CoA binding protein in tetragonal crystal form Deposited 2001-04-12 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 1–86（86 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；25% PEG5000 MME, 40MM NI(SO4)2, 40MM HEPES PH7.5, pH 7.50
Resolution 2.00 Å R-free 0.255
1NTI RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP Deposited 2003-01-30 Different ligand/ion Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–86（86 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；310 K；Ionic strength (raw mmCIF value) no salt added；Pressure ambient
NMR sample composition 0.5mM recombinant bovine ACBP, 5% 3:1 [DMPC:DHPC], pH 6.5 | 10% D2O, 90% H2O
NMR sample composition 0.5mM recombinant bovine ACBP, pH 6.5 | 10% D2O, 90% H2O
Resolution not provided
1NVL RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP, in complex with palmitoyl-coenzyme A Deposited 2003-02-04 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–86（86 aa）
Not recorded COA COENZYME A × 1 PLM PALMITIC ACID × 1 SOLUTION NMR
NMR measurement conditions pH 6.5；310 K；Ionic strength (raw mmCIF value) no salt added；Pressure ambient
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) no salt added；Pressure ambient
NMR sample composition 0.5 mM ACBP, pH 6.5, 0.5 mM palmitoyl-coenzyme A, 5% (3:1) [DMPC:DHPC], 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM ACBP, pH 6.5, 0.5 mM palmitoyl-coenzyme A, 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
2ABD THE THREE-DIMENSIONAL STRUCTURE OF ACYL-COENZYME A BINDING PROTEIN FROM BOVINE LIVER. STRUCTURAL REFINEMENT USING HETERONUCLEAR MULTIDIMENSIONAL NMR SPECTROSCOPY Deposited 1993-03-05 Different ligand/ion Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–86（86 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K
Resolution not provided

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACBP_BOVIN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–86； UniProt 1–86

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 1aca

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1aca
Deposition date deposition_date1992-11-17
Structure title titleTHREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN ACYL-COENZYME A BINDING PROTEIN AND PALMITOYL-COENZYME A
Keywords keywordsACYL-COENZYME A BINDING PROTEIN; ACYL-COENZYME A BINDING 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_guinier12.41 Å
Radius of gyration Rg (electron density) rg_electron12.22 Å
Forward intensity I(0) i0670457000.00
Molecular weight molecular_weight218380.0 kDa
Excluded volume excluded_volume272640 ų
Envelope volume envelope_volume19966 ų
Hydration-shell volume shell_volume12211 ų
Envelope diameter envelope_diameter48.7 Å
Shell Rg shell_rg19.67 Å
Envelope Rg envelope_rg14.16 Å
Shape Rg shape_rg12.19 Å
Total Rg total_rg12.47 Å
Total atoms total_atoms30360
Residues n_residues1720
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 dmax41.1 Å
Rg (real space) rg_real12.32 Å
Rg uncertainty (real space) rg_real_error0.26 Å
I(0) (real space) i0_real6.7050e+08
I(0) uncertainty (real space) i0_real_error7.2080e+06
Rg (reciprocal space) rg_reciprocal12.33 Å
I(0) (reciprocal space) i0_reciprocal670500000.0000
Solution quality estimate total_estimate0.8784
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.6 Å
Skewness Skewness skewness0.086
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha221600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.985
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1acaa_
Class classa — All alpha proteins
Fold Fold folda.11 — Acyl-CoA binding protein-like
Superfamily Superfamily superfamilya.11.1 — Acyl-CoA binding protein
Family Family familya.11.1.1 — Acyl-CoA binding protein

CATH v4.4 (1 domains)

Domain ID domain_id1acaA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology80 — Acyl-CoA Binding Protein
Homologous superfamily homologous superfamily10 —
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8. Citations (4)

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9. Files and Curves (10)