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Structure paper

TitleMutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer.
Journal, issue, pagesBiochemistry, Vol. 51, Page 9857-9868, Year 2012
Publish dateJul 13, 2012 (structure data deposition date)
AuthorsSmith, K.W. / Stroupe, M.E.
External linksBiochemistry / PubMed:23153334
MethodsX-ray diffraction
Resolution1.56 - 2.4 Å
Structure data

PDB-4g38:
Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer
Method: X-RAY DIFFRACTION / Resolution: 1.56 Å

PDB-4g39:
Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-4htr:
N149W variant of SiRHP bound to sulfite
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-K:
Unknown entry

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-SRM:
SIROHEME

ChemComp-HOH:
WATER

ChemComp-SO3:
SULFITE ION

ChemComp-NA:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE / SNiRR / sulfite reductase flavoprotein / oxidoreductase/substrate / siroheme-binding protein / iron-sulfur cluster / S/NiRR / oxidoreductase-substrate complex

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