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Structure paper

TitleRole of a Conserved Glutamine Residue in Tuning the Catalytic Activity of Escherichia coli Cytochrome c Nitrite Reductase.
Journal, issue, pagesBiochemistry, Vol. 47, Page 3789-3799, Year 2008
Publish dateSep 25, 2007 (structure data deposition date)
AuthorsClarke, T.A. / Kemp, G.L. / Wonderen, J.H. / Doyle, R.M. / Cole, J.A. / Tovell, N. / Cheesman, M.R. / Butt, J.N. / Richardson, D.J. / Hemmings, A.M.
External linksBiochemistry / PubMed:18311941
MethodsX-ray diffraction
Resolution1.74 - 2.04 Å
Structure data

PDB-2rdz:
High Resolution Crystal Structure of the Escherichia coli Cytochrome c Nitrite Reductase.
Method: X-RAY DIFFRACTION / Resolution: 1.74 Å

PDB-2rf7:
Crystal structure of the escherichia coli nrfa mutant Q263E
Method: X-RAY DIFFRACTION / Resolution: 2.04 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HEC:
HEME C

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • escherichia coli k12 (bacteria)
KeywordsOXIDOREDUCTASE / decaheme / reductase / Electron transport / Iron / Metal-binding / Transport / calcium ligand / Heme / Periplasm

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