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1KQ0

Human methionine aminopeptidase type II in complex with D-methionine

Summary for 1KQ0
Entry DOI10.2210/pdb1kq0/pdb
Related1KQ9
DescriptorMethionine aminopeptidase 2, ZINC ION, D-METHIONINE, ... (5 entities in total)
Functional Keywordscentral b-sheet and two pairs of a-helices, hydrolase
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight53339.70
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 citationNonato, 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: 16540317
DOI: 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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