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. 2019 Apr 17;5(4):eaav4310. doi: 10.1126/sciadv.aav4310

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Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).

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Fig. 3 — (A) Close-up of the active site. Three monomers, shown in different colors, contribute side chains to the active-site cavity, such as the conserved Asp²⁵⁵/His²⁵⁶ pair from one monomer and the N-terminal Val^33′ from another. The active-site heme 4 is bound covalently to Tyr^462″ from a third monomer, as well as to the conserved Cys²⁰² in addition to the two cysteines of the heme-binding motif (in the background). (B) Sliced view of the HDH complex. Heme groups 3 of each monomer are solvent-exposed just inside the holes, leading to the central cavity in the complex.