1bn5
From Proteopedia
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|PDB= 1bn5 |SIZE=350|CAPTION= <scene name='initialview01'>1bn5</scene>, resolution 1.8Å | |PDB= 1bn5 |SIZE=350|CAPTION= <scene name='initialview01'>1bn5</scene>, resolution 1.8Å | ||
|SITE= <scene name='pdbsite=CO2:Dicobalt+Active+Site'>CO2</scene> | |SITE= <scene name='pdbsite=CO2:Dicobalt+Active+Site'>CO2</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> | + | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU</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=1bn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bn5 OCA], [http://www.ebi.ac.uk/pdbsum/1bn5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bn5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Liu, S.]] | [[Category: Liu, S.]] | ||
[[Category: Widom, J.]] | [[Category: Widom, J.]] | ||
| - | [[Category: CO]] | ||
| - | [[Category: TBU]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: methionine aminopeptidase]] | [[Category: methionine aminopeptidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:04:17 2008'' |
Revision as of 16:04, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| 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
Overview
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 Structure
1BN5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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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