Methionine aminopeptidase 1 is an enzyme that in humans is encoded by the METAP1gene. This enzyme is a methionyl aminopeptidase which cleaves the N-terminal methionine from precursor proteins, with particular affinity for when the second amino acid is small and non-charged. Also important for the normal functioning of the cell cycle. This enzyme uses metal cations as a cofactor (making it a metalloprotein), but which one is used in the body remains debated.
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2b3h: Crystal structure of Human Methionine Aminopeptidase Type I with a third cobalt in the active site
2b3k: Crystal structure of Human Methionine Aminopeptidase Type I in the holo form
2b3l: Crystal structure of type I human methionine aminopeptidase in the apo form
2g6p: Crystal structure of truncated (delta 1-89) human methionine aminopeptidase Type 1 in complex with Pyridyl pyrimidine derivative
2gz5: Human Type 1 methionine aminopeptidase in complex with ovalicin at 1.1 Ang
2nq6: Crystal structure of human methionine aminopeptidase type 1 in complex with 3-tert-Butoxycarbonylaminopyridine-2-carboxylic acid thiazole-2-ylamide
2nq7: Crystal structure of type 1 human methionine aminopeptidase in complex with 3-(2,2-Dimethylpropionylamino)pyridine-2-carboxylic acid thiazole-2-ylamide