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1.14.15.1
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the camphor-free structure is in an open conformation characterized by a water-filled channel created by the retraction of the F and G helices, disorder of the B' helix, and loss of the K+ binding. site. Presence of K+ alone does not alter the open conformation, while camphor alone is sufficient for closure of the channel
711234
1.14.15.1
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three-dimensional structure and dynamics of the open and closed states of CYP101A1, NMR analysis and molecular dynamics simulations, overview
711268
1.14.15.1
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wild-type dioxygen complex structure: high occupancy and a ordered structure of the iron-linked dioxygen and two 'catalytic' water molecules that form part of a proton relay system to the iron-linked dioxygen
674474
1.14.15.1
tetramer
crystallization data
657898
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