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TitleExperimental and theoretical study on converting myoglobin into a stable domain-swapped dimer by utilizing a tight hydrogen bond network at the hinge region.
Journal, issue, pagesRsc Adv, Vol. 11, Page 37604-37611, Year 2021
Publish dateAug 17, 2021 (structure data deposition date)
AuthorsXie, C. / Shimoyama, H. / Yamanaka, M. / Nagao, S. / Komori, H. / Shibata, N. / Higuchi, Y. / Shigeta, Y. / Hirota, S.
External linksRsc Adv / PubMed:35496441
MethodsX-ray diffraction
Resolution1.16 - 1.39 Å
Structure data

PDB-7v5p:
The dimeric structure of G80A/H81A myoglobin
Method: X-RAY DIFFRACTION / Resolution: 1.16 Å

PDB-7v5q:
The dimeric structure of G80A/H81A/L137E myoglobin
Method: X-RAY DIFFRACTION / Resolution: 1.38 Å

PDB-7v5r:
The dimeric structure of G80A/H81A/L137D myoglobin
Method: X-RAY DIFFRACTION / Resolution: 1.39 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-O:
OXYGEN ATOM

ChemComp-HOH:
WATER

Source
  • equus caballus (horse)
KeywordsOXYGEN BINDING / OXYGEN STORAGE

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