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TitlePro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding.
Journal, issue, pagesNat Commun, Vol. 9, Page 512-512, Year 2018
Publish dateSep 6, 2017 (structure data deposition date)
AuthorsGuo, H.F. / Tsai, C.L. / Terajima, M. / Tan, X. / Banerjee, P. / Miller, M.D. / Liu, X. / Yu, J. / Byemerwa, J. / Alvarado, S. ...Guo, H.F. / Tsai, C.L. / Terajima, M. / Tan, X. / Banerjee, P. / Miller, M.D. / Liu, X. / Yu, J. / Byemerwa, J. / Alvarado, S. / Kaoud, T.S. / Dalby, K.N. / Bota-Rabassedas, N. / Chen, Y. / Yamauchi, M. / Tainer, J.A. / Phillips, G.N. / Kurie, J.M.
External linksNat Commun / PubMed:29410444
MethodsX-ray diffraction
Resolution2.002 - 2.241 Å
Structure data

PDB-6ax6:
The crystal structure of a lysyl hydroxylase from Acanthamoeba polyphaga mimivirus
Method: X-RAY DIFFRACTION / Resolution: 2.241 Å

PDB-6ax7:
The crystal structure of a lysyl hydroxylase from Acanthamoeba polyphaga mimivirus
Method: X-RAY DIFFRACTION / Resolution: 2.002 Å

Chemicals

ChemComp-IOD:
IODIDE ION

ChemComp-FE2:
Unknown entry

ChemComp-HOH:
WATER

Source
  • acanthamoeba polyphaga mimivirus
KeywordsOXIDOREDUCTASE / double-stranded ?-helix / dimer / dioxygenase / collagen

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