1c5b
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1c5c|1C5C]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c5b OCA], [http://www.ebi.ac.uk/pdbsum/1c5b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c5b RCSB]</span> | ||
}} | }} | ||
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[[Category: unliganded]] | [[Category: unliganded]] | ||
| - | ''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 19:14:45 2008'' |
Revision as of 16:14, 30 March 2008
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| , resolution 2.10Å | |||||||
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| Related: | 1C5C
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DECARBOXYLASE CATALYTIC ANTIBODY 21D8 UNLIGANDED FORM
Overview
Antibody 21D8 catalyzes the solvent-sensitive decarboxylation of 3-carboxybenzisoxazoles. The crystal structure of chimeric Fab 21D8 with and without hapten at 1.61 A and 2.10 A, respectively, together with computational analysis, shows how a melange of polar and non-polar sites are exploited to achieve both substrate binding and acceleration of a reaction normally facilitated by purely aprotic dipolar media. The striking similarity of the decarboxylase and a series of unrelated esterase antibodies also highlights the chemical versatility of structurally conserved anion binding sites and the relatively subtle changes involved in fine-tuning the immunoglobulin pocket for recognition of different ligands and catalysis of different reactions.
About this Structure
1C5B is a Protein complex structure of sequences from Mus musculus + homo sapiens. Full crystallographic information is available from OCA.
Reference
Catalysis of decarboxylation by a preorganized heterogeneous microenvironment: crystal structures of abzyme 21D8., Hotta K, Lange H, Tantillo DJ, Houk KN, Hilvert D, Wilson IA, J Mol Biol. 2000 Oct 6;302(5):1213-25. PMID:11183784
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