Role of the biradical intermediate observed during the turnover of SLAC: A two-domain laccase from Streptomyces coelicolor
The structure was published by Gupta, A., Nederlof, I., Sottini, S., et al., Groenen, E.J., Thomassen, E.A., and Canters, G.W., in 2012 in a paper entitled "Involvement of Tyr108 in the enzyme mechanism of the small laccase from Streptomyces coelicolor" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.734 Å and deposited in 2012.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Putative copper oxidase.
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 homotrimers.
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: