› 2abd

Solution NMR

THE THREE-DIMENSIONAL STRUCTURE OF ACYL-COENZYME A BINDING PROTEIN FROM BOVINE LIVER. STRUCTURAL REFINEMENT USING HETERONUCLEAR MULTIDIMENSIONAL NMR SPECTROSCOPY

Released:
DOI: 10.2210/pdb2abd/pdb
PDB entry 2abd coloured by chain, ensemble of 29 models, front view.
PDB entry 2abd coloured by chain, ensemble of 29 models, side view.
PDB entry 2abd coloured by chain, ensemble of 29 models, top view.
Source organism: Bos taurus
Primary publication:
The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy.
Andersen KV, Poulsen FM
J Biomol NMR 3 271-84 (1993)
PMID: 8358232

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139376 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-CoA-binding protein Chain: A
Molecule details ›
Chain: A
Length: 86 amino acids
Theoretical weight: 9.93 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07107 (Residues: 2-87; Coverage: 99%)
Gene name: DBI
Sequence domains: Acyl CoA binding protein
Structure domains: Acyl-CoA Binding Protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

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Citations

4 review citations

Macromolecular modeling with rosetta.
Das et al. (2008)
3 more

32 mentions without citation

What lessons can be learned from studying the folding of homologous proteins?
Nickson et al. (2010)
31 more