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Structure paper

TitleResidue F4 plays a key role in modulating oxygen affinity and cooperativity in Scapharca dimeric hemoglobin
Journal, issue, pagesBiochemistry, Vol. 44, Page 14419-14430, Year 2005
Publish dateAug 28, 2005 (structure data deposition date)
AuthorsKnapp, J.E. / Bonham, M.A. / Gibson, Q.H. / Nichols, J.C. / Royer Jr., W.E.
External linksBiochemistry / PubMed:16262242
MethodsX-ray diffraction
Resolution1.5 - 2.3 Å
Structure data

PDB-2auo:
Residue F4 plays a key role in modulating the oxygen affinity and cooperatrivity in Scapharca dimeric hemoglobin
Method: X-RAY DIFFRACTION / Resolution: 1.53 Å

PDB-2aup:
Residue F4 plays a key role in modulating oxygen affinity and cooperativity in Scapharca dimeric hemoglobin
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2auq:
HbI (F97V) CO bound
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2aur:
F97V (no ligand bound)
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-2av0:
F97L with CO bound
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-2av3:
F97L- no ligand
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-CMO:
CARBON MONOXIDE

ChemComp-HOH:
WATER

Source
  • scapharca inaequivalvis (ark clam)
KeywordsOXYGEN STORAGE/TRANSPORT / oxygen transport / allostery / oxygen affinity / OXYGEN STORAGE-TRANSPORT COMPLEX / oxygen binding / cooperative hemoglobin / hemoglobin / allosteric

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