1KQ0
Human methionine aminopeptidase type II in complex with D-methionine
Summary for 1KQ0
Entry DOI | 10.2210/pdb1kq0/pdb |
Related | 1KQ9 |
Descriptor | Methionine aminopeptidase 2, ZINC ION, D-METHIONINE, ... (5 entities in total) |
Functional Keywords | central b-sheet and two pairs of a-helices, hydrolase |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 1 |
Total formula weight | 53339.70 |
Authors | Nonato, M.C.,Widom, J.,Clardy, J. (deposition date: 2002-01-03, release date: 2003-12-09, Last modification date: 2023-08-16) |
Primary citation | Nonato, M.C.,Widom, J.,Clardy, J. Human methionine aminopeptidase type 2 in complex with L- and D-methionine Bioorg.Med.Chem.Lett., 16:2580-2583, 2006 Cited by PubMed Abstract: Human methionine aminopeptidase type 2 (hMetAP-2) was identified as the molecular target of anti-angiogenic agents such as fumagillin and its analogues. We describe here the crystal structure of hMetAP-2 in complex with l-methionine and d-methionine at 1.9 and 2.0A resolution, respectively. The comparison of the structure of the two complexes establishes the basis of enantiomer discrimination and provides some considerations for the design of selective MetAP-2 inhibitors. PubMed: 16540317DOI: 10.1016/j.bmcl.2006.02.047 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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