1YEE: Structure Of A Catalytic Antibody, Igg2a Fab Fragment (D2.5)

The x-ray structures of three esterase-like catalytic antibodies identified by screening for catalytic activity the entire hybridoma repertoire, elicited in response to a phosphonate transition state analog (TSA) hapten, were analyzed. The high resolution structures account for catalysis by transition state stabilization, and in all three antibodies a tyrosine residue participates in the oxyanion hole. Despite significant conformational differences in their combining sites, the three antibodies, which are the most efficient among those elicited, achieve catalysis in essentially the same mode, suggesting that evolution for binding to a single TSA followed by screening for catalysis lead to antibodies with structural convergence.
PDB ID: 1YEEDownload
MMDB ID: 6678
PDB Deposition Date: 1997/4/15
Updated in MMDB: 1998/11
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 1YEE: dimeric; determined by author and by software (PISA)
Molecular Components in 1YEE
Label Count Molecule
Proteins (2 molecules)
Igg2a FAB Fragment (D2.5)
Molecule annotation
Igg2a FAB Fragment (D2.5)(Gene symbol: Ighg2a)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB