SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY
The structure was published by Roberts, E.L., Shu, N., Howard, M.J., et al., Morris, T., Cronan Jr., J.E., and Perham, R.N., in 1999 in a paper entitled "Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy." (abstract).
The structure was determined using NMR spectroscopy and deposited in 1999.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of PROTEIN (ACETYL-COA CARBOXYLASE). This molecule has the UniProt identifier P0ABD8 (BCCP_ECOLI). The sample contained 80 residues which is < 90% of the natural sequence. Out of 80 residues 80 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: