Crystal structure of tt0168 from Thermus thermophilus HB8
The structure was published by Hisanaga, Y., Ago, H., Nakagawa, N., et al., Kuramitsu, S., Yokoyama, S., and Miyano, M., in 2004 in a paper entitled "Structural Basis of the Substrate-specific Two-step Catalysis of Long Chain Fatty Acyl-CoA Synthetase Dimer" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2003.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of long-chain-fatty-acid-CoA synthetase.
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 most likely forms homodimers.
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: