6L2U

Soluble methane monooxygenase reductase FAD-binding domain from Methylosinus sporium.

Summary for 6L2U

• Entry DOI: 10.2210/pdb6l2u/pdb
• Descriptor: Methane monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: metal-binding, redoxreaction, oxidoreductase
• Biological source: Methylosinus sporium
• Total number of polymer chains: 2
• Total formula weight: 24036.41

Authors

Park, J.H.,Ha, S.C.,Rao, Z.,Yoo, H.,Yoon, C.,Kim, S.Y.,Kim, D.S.,Lee, S.J. (deposition date: 2019-10-07, release date: 2021-03-03, Last modification date: 2024-05-29)

Primary citation

Lee, C.,Ha, S.C.,Rao, Z.,Hwang, Y.,Kim, D.S.,Kim, S.Y.,Yoo, H.,Yoon, C.,Na, J.G.,Park, J.H.,Lee, S.J.
Elucidation of the electron transfer environment in the MMOR FAD-binding domain from Methylosinus sporium 5.
Dalton Trans, 50:16493-16498, 2021

PubMed Abstract: By facilitating electron transfer to the hydroxylase diiron center, MMOR-a reductase-serves as an essential component of the catalytic cycle of soluble methane monooxygenase. Here, the X-ray structure analysis of the FAD-binding domain of MMOR identified crucial residues and its influence on the catalytic cycle.

PubMed: 34734616
DOI: 10.1039/d1dt03273a

Experimental method

X-RAY DIFFRACTION (1.5 Å)