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TitlePositive and negative cooperativities at subsequent steps of oxygenation regulate the allosteric behavior of multistate sebacylhemoglobin.
Journal, issue, pagesBiochemistry, Vol. 35, Page 3418-3425, Year 1996
Publish dateAug 29, 1995 (structure data deposition date)
AuthorsBucci, E. / Razynska, A. / Kwansa, H. / Gryczynski, Z. / Collins, J.H. / Fronticelli, C. / Unger, R. / Braxenthaler, M. / Moult, J. / Ji, X. / Gilliland, G.
External linksBiochemistry / PubMed:8639491
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-1cls:
CROSS-LINKED HUMAN HEMOGLOBIN DEOXY
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-O:
OXYGEN ATOM

ChemComp-SO4:
SULFATE ION

ChemComp-DEC:
SEBACIC ACID

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsOXYGEN TRANSPORT / HEMOGLOBIN / HUMAN / DEOXY / CROSS-LINKED

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