CATH Domain 1yw9A01

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.90	Alpha-Beta Complex
	3.90.230	Creatine Amidinohydrolase
	3.90.230.10	Creatinase/methionine aminopeptidase superfamily

Domain Context

CATH Clusters

Superfamily	Creatinase/methionine aminopeptidase superfamily
Functional Family	Methionine aminopeptidase 2

Enzyme Information

3.4.11.18

Methionyl aminopeptidase.

based on mapping to UniProt P50579

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.

-!- This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides. -!- The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val). -!- Belongs to peptidase family M24A.

UniProtKB Entries (1)

P50579

MAP2_HUMAN

Homo sapiens

Methionine aminopeptidase 2

PDB Structure

PDB	1YW9
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Discovery and optimization of anthranilic acid sulfonamides as inhibitors of methionine aminopeptidase-2: a structural basis for the reduction of albumin binding. Sheppard, G.S., Wang, J., Kawai, M., Fidanze, S.D., BaMaung, N.Y., Erickson, S.A., Barnes, D.M., Tedrow, J.S., Kolaczkowski, L., Vasudevan, A., Park, D.C., Wang, G.T., Sanders, W.J., Mantei, R.A., Palazzo, F., Tucker-Garcia, L., Lou, P., Zhang, Q., Park, C.H., Kim, K.H., Petros, A., Olejniczak, E., Nettesheim, D., Hajduk, P., Henkin, J., Lesniewski, R., Davidsen, S.K., Bell, R.L. J.Med.Chem.