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Structure paper

TitleSymmetry-related residues as promising hotspots for the evolution of de novo oligomeric enzymes.
Journal, issue, pagesChem Sci, Vol. 12, Page 5091-5101, Year 2021
Publish dateNov 21, 2019 (structure data deposition date)
AuthorsYu, J. / Yang, J. / Seok, C. / Song, W.J.
External linksChem Sci / PubMed:34168770
MethodsX-ray diffraction
Resolution1.98 - 2.45 Å
Structure data

PDB-6lde:
Crystal structure of the Zn-directed tetramer of the engineered cyt cb 562 variant, C96V AB5
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-6ldf:
Crystal structure of the Zn-directed tetramer of the engineered cyt cb 562 variant, C96K AB5
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

PDB-6ldg:
Crystal structure of the Zn-directed tetramer of the engineered cyt cb 562 variant, C96I AB5
Method: X-RAY DIFFRACTION / Resolution: 1.98 Å

PDB-7dcl:
Crystal structure of the Zn-directed tetramer of the engineered cyt cb 562 variant, C96I/A38S AB5
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

Chemicals

ChemComp-HEC:
HEME C

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsELECTRON TRANSPORT / Artificial enzyme / Metallohydrolase / Directed evolution / METAL BINDING PROTEIN

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