Extended Data Fig. 6: Structures of four HKASs in complex with ThDP cofactors. | Nature Chemistry

Extended Data Fig. 6: Structures of four HKASs in complex with ThDP cofactors.

From: Structural insights into two thiamine diphosphate-dependent enzymes and their synthetic applications in carbon–carbon linkage reactions

Extended Data Fig. 6

a, The structure of CsmA-ThDP with two monomer molecules in one asymmetric unit. b, Amplified region of the ThDP (yellow stick) binding site in CsmA. c, Amplified region of the ADP (magenta stick) binding site in CsmA. d, The structure of BbmA-ThDP with two monomer molecules in one asymmetric unit. e, Amplified region of the ThDP (yellow stick) binding site in BbmA. f, Amplified region of the ADP (magenta stick) binding site in BbmA. g, The structure of AtAHAS with two monomer molecules in one asymmetric unit. h, Amplified region of the ThDP (yellow stick) binding site in AtAHAS. i, Amplified region of the FAD (cyan stick) binding site in AtAHAS. j, The structure of AlsS with two monomer molecules in one asymmetric unit. k, Amplified region of the ThDP (yellow stick) binding site in AlsS. l, Amplified region of the site (no FAD or ADP binding) in AlsS corresponding to the ADP binding site in CsmA and BbmA.

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