1b6a: Difference between revisions

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|PDB= 1b6a |SIZE=350|CAPTION= <scene name='initialview01'>1b6a</scene>, resolution 1.60&Aring;
|PDB= 1b6a |SIZE=350|CAPTION= <scene name='initialview01'>1b6a</scene>, resolution 1.60&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> and <scene name='pdbligand=TN4:(CHLOROACETYL)CARBAMIC ACID (3R,4S,5S,5R)-5-METHOXY-4-[(2R,3R)-2-METHYL-3-(3-METHYL-2-BUTENYL)OXIRANYL]-1-OXASPIRO[2.5]OCT-6-YL ESTER'>TN4</scene>
|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=TN4:(CHLOROACETYL)CARBAMIC+ACID+(3R,4S,5S,5R)-5-METHOXY-4-[(2R,3R)-2-METHYL-3-(3-METHYL-2-BUTENYL)OXIRANYL]-1-OXASPIRO[2.5]OCT-6-YL+ESTER'>TN4</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18]  
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b6a OCA], [http://www.ebi.ac.uk/pdbsum/1b6a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b6a RCSB]</span>
}}
}}


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[[Category: Clardy, J C.]]
[[Category: Clardy, J C.]]
[[Category: Liu, S.]]
[[Category: Liu, S.]]
[[Category: CO]]
[[Category: TN4]]
[[Category: aminopeptidase]]
[[Category: aminopeptidase]]
[[Category: angiogenesis inhibitor]]
[[Category: angiogenesis inhibitor]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:06:50 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:54:27 2008''

Revision as of 18:54, 30 March 2008

File:1b6a.gif


PDB ID 1b6a

Drag the structure with the mouse to rotate
, resolution 1.60Å
Ligands: ,
Activity: Methionyl aminopeptidase, with EC number 3.4.11.18
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



HUMAN METHIONINE AMINOPEPTIDASE 2 COMPLEXED WITH TNP-470


OverviewOverview

The fungal metabolite fumagillin suppresses the formation of new blood vessels, and a fumagillin analog is currently in clinical trials as an anticancer agent. The molecular target of fumagillin is methionine aminopeptidase-2 (MetAP-2). A 1.8 A resolution crystal structure of free and inhibited human MetAP-2 shows a covalent bond formed between a reactive epoxide of fumagillin and histidine-231 in the active site of MetAP-2. Extensive hydrophobic and water-mediated polar interactions with other parts of fumagillin provide additional affinity. Fumagillin-based drugs inhibit MetAP-2 but not MetAP-1, and the three-dimensional structure also indicates the likely determinants of this specificity. The structural basis for fumagillin's potency and specificity forms the starting point for structure-based drug design.

About this StructureAbout this Structure

1B6A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of human methionine aminopeptidase-2 complexed with fumagillin., Liu S, Widom J, Kemp CW, Crews CM, Clardy J, Science. 1998 Nov 13;282(5392):1324-7. PMID:9812898

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