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Structure paper

TitleThe Role of Glu498 in the Dioxygen Reactivity of Cota-Laccase from Bacillus Subtilis.
Journal, issue, pagesDalton Trans, Vol. 39, Page 2875-, Year 2010
Publish dateFeb 28, 2012 (structure data deposition date)
AuthorsChen, Z. / Durao, P. / Silva, C.S. / Pereira, M.M. / Todorovic, S. / Hildebrandt, P. / Bento, I. / Lindley, P.F. / Martins, L.O.
External linksDalton Trans / PubMed:20200715
MethodsX-ray diffraction
Resolution1.7 - 2.1 Å
Structure data

PDB-4ako:
Mutations in the neighbourhood of CotA-laccase trinuclear site: E498L mutant
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-4akp:
Mutations in the neighbourhood of CotA-laccase trinuclear site: E498T mutant
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-4akq:
Mutations in the neighbourhood of CotA-laccase trinuclear site: E498D mutant
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-OXY:
OXYGEN MOLECULE

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • bacillus subtilis (bacteria)
KeywordsOXIDOREDUCTASE / MULTI-COPPER OXIDASE / TRINUCLEAR CLUSTER / OXYGEN REDUCTION / TRINUCLEAR CLUSTER OXYGEN REDUCTION / COTA-LACCASE

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