6Q29
Crystal structure of Laccase from Thermus thermophilus HB27 with an open conformation of beta-hairpin (Average deposted dose 2.5 MGy)
Summary for 6Q29
Entry DOI | 10.2210/pdb6q29/pdb |
Descriptor | Laccase, TETRAETHYLENE GLYCOL, TRIETHYLENE GLYCOL, ... (5 entities in total) |
Functional Keywords | open loop, multicopper oxidase, structural protein |
Biological source | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) |
Total number of polymer chains | 1 |
Total formula weight | 49262.95 |
Authors | Miranda-Blancas, R.,Rudino-Pinera, E. (deposition date: 2019-08-07, release date: 2020-08-12, Last modification date: 2023-10-11) |
Primary citation | Miranda-Blancas, R.,Avelar, M.,Rodriguez-Arteaga, A.,Sinicropi, A.,Rudino-Pinera, E. The beta-hairpin from the Thermus thermophilus HB27 laccase works as a pH-dependent switch to regulate laccase activity. J.Struct.Biol., 213:107740-107740, 2021 Cited by PubMed: 33962016DOI: 10.1016/j.jsb.2021.107740 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.702 Å) |
Structure validation
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