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Fig. 3 | Biology Direct

Fig. 3

From: Functional and structural characterization of the human indolethylamine N-methyltransferase through fluorometric, thermal and computational docking analyses

Fig. 3

Structural features of hINMT. A Structure overview of hINMT (PDB code 2A14, unpublished) showing the protein fold, the binding site of SAH (pink) and its ligands (in sticks). B The “cap”, N-terminal, central and C-terminal domains proposed for hINMT, based on the similarity to related proteins, i.e., NNMT from humans (PDB code 5YJF), mice (PDB code 5XVK) and monkeys (PDB code 5XVQ). C The four non-conserved cysteine residues in hINMT (in sticks). Due to their proximity, Cys213 and Cys168 probably create a disulfide bond. Alike, Cys254 and Cys44 can bind covalently

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Biology Direct

ISSN: 1745-6150

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