1C5B

DECARBOXYLASE CATALYTIC ANTIBODY 21D8 UNLIGANDED FORM

Summary for 1C5B

• Entry DOI: 10.2210/pdb1c5b/pdb
• Related: 1C5C
• Descriptor: CHIMERIC DECARBOXYLASE ANTIBODY 21D8 (3 entities in total)
• Functional Keywords: immunoglobulin, catalytic antibody, chimeric fab, decarboxylase, unliganded, immune system
• Biological source: Mus musculus, Homo sapiens (house mouse, human); More
• Total number of polymer chains: 2
• Total formula weight: 46520.92

Authors

Hotta, K.,Wilson, I.A. (deposition date: 1999-11-08, release date: 2000-10-11, Last modification date: 2023-08-09)

Primary citation

Hotta, K.,Lange, H.,Tantillo, D.J.,Houk, K.N.,Hilvert, D.,Wilson, I.A.
Catalysis of decarboxylation by a preorganized heterogeneous microenvironment: crystal structures of abzyme 21D8.
J.Mol.Biol., 302:1213-1225, 2000

PubMed Abstract: 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.

PubMed: 11183784
DOI: 10.1006/jmbi.2000.4503

Experimental method

X-RAY DIFFRACTION (2.1 Å)