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TitleThe nitrite anion binds to human hemoglobin via the uncommon O-nitrito mode.
Journal, issue, pagesBiochemistry, Vol. 47, Page 8247-8249, Year 2008
Publish dateMay 21, 2008 (structure data deposition date)
AuthorsYi, J. / Safo, M.K. / Richter-Addo, G.B.
External linksBiochemistry / PubMed:18630930
MethodsX-ray diffraction
Resolution1.8 Å
Structure data

PDB-3d7o:
Human hemoglobin, nitrogen dioxide anion modified
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-NO2:
NITRITE ION

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-MBN:
TOLUENE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsOXYGEN TRANSPORT / Human Hemoglobin / Acetylation / Disease mutation / Glycation / Glycoprotein / Heme / Iron / Metal-binding / Polymorphism / Transport / Hypotensive agent / Pyruvate / S-nitrosylation / Vasoactive

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