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TitleThe role of positive charged residue in the proton-transfer mechanism of two-domain laccase from Streptomyces griseoflavus Ac-993.
Journal, issue, pagesJ. Biomol. Struct. Dyn., Vol. 40, Page 8324-8331, Year 2022
Publish dateJun 26, 2020 (structure data deposition date)
AuthorsGabdulkhakov, A. / Kolyadenko, I. / Oliveira, P. / Tamagnini, P. / Mikhaylina, A. / Tishchenko, S.
External linksJ. Biomol. Struct. Dyn. / PubMed:33870857
MethodsX-ray diffraction
Resolution1.6 - 2.05 Å
Structure data

PDB-6zij:
Crystal Structure of Two-Domain Laccase mutant R240H from Streptomyces griseoflavus
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-6zip:
Crystal Structure of Two-Domain Laccase mutant R240A from Streptomyces griseoflavus
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-GOL:
GLYCEROL

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-OXY:
OXYGEN MOLECULE

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PER:
PEROXIDE ION

Source
  • streptomyces griseoflavus (bacteria)
KeywordsOXIDOREDUCTASE / Two-Domain Laccase / laccase / Streptomyces griseoflavus

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