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Structure paper

TitleThe structure of a deoxygenated 400 kDa haemoglobin reveals ternary- and quaternary-structural changes of giant haemoglobins
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 70, Page 1823-1831, Year 2014
Publish dateJun 1, 2013 (structure data deposition date)
AuthorsNumoto, N. / Nakagawa, T. / Ohara, R. / Hasegawa, T. / Kita, A. / Yoshida, T. / Maruyama, T. / Imai, K. / Fukumori, Y. / Miki, K.
External linksActa Crystallogr. ,Sect. D / PubMed:25004960
MethodsX-ray diffraction
Resolution2.4 - 2.9 Å
Structure data

PDB-3wct:
The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: Oxygenated form
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-3wcu:
The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: Deoxygenated form
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-3wcv:
The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: CA bound form
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3wcw:
The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: MG bound form
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-OXY:
OXYGEN MOLECULE

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

Source
  • lamellibrachia satsuma (invertebrata)
KeywordsOXYGEN TRANSPORT / globin fold / oxygen binding / blood

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