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Structure paper

TitleStructural characterization of the nitrogenase molybdenum-iron protein with the substrate acetylene trapped near the active site.
Journal, issue, pagesJ. Inorg. Biochem., Vol. 180, Page 129-134, Year 2017
Publish dateOct 18, 2017 (structure data deposition date)
AuthorsKeable, S.M. / Vertemara, J. / Zadvornyy, O.A. / Eilers, B.J. / Danyal, K. / Rasmussen, A.J. / De Gioia, L. / Zampella, G. / Seefeldt, L.C. / Peters, J.W.
External linksJ. Inorg. Biochem. / PubMed:29275221
MethodsX-ray diffraction
Resolution1.68 Å
Structure data

PDB-6bbl:
Crystal structure of the a-96Gln MoFe protein variant in the presence of the substrate acetylene
Method: X-RAY DIFFRACTION / Resolution: 1.68 Å

Chemicals

ChemComp-C2H:
acetylene

ChemComp-IMD:
IMIDAZOLE

ChemComp-HCA:
3-HYDROXY-3-CARBOXY-ADIPIC ACID

ChemComp-ICS:
iron-sulfur-molybdenum cluster with interstitial carbon

ChemComp-1CL:
FE(8)-S(7) CLUSTER, OXIDIZED

ChemComp-FE:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • azotobacter vinelandii (bacteria)
KeywordsOXIDOREDUCTASE / ELECTRON TRANSPORT / Nitrogenase / N2 reduction / FeMo-cofactor / substrate binding / acetylene

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