From mmconn[ AT ]silibone.cchem.berkeley.edu Wed Nov 29 13:39:04 1995 Received: from hydrogen.CChem.Berkeley.EDU for mmconn %-% at %-% silibone.cchem.berkeley.edu by www.ccl.net (8.6.10/950822.1) id NAA15973; Wed, 29 Nov 1995 13:32:52 -0500 Received: from silibone.cchem.berkeley.edu by hydrogen.CChem.Berkeley.EDU (8.6.10/1.41) id KAA12174; Wed, 29 Nov 1995 10:32:52 -0800 Received: by silibone.cchem.berkeley.edu (920330.SGI/920502.SGI.AUTO) for : at :hydrogen.cchem.berkeley.edu:chemistry: at :www.ccl.net id AA15628; Wed, 29 Nov 95 10:29:12 -0800 Date: Wed, 29 Nov 95 10:29:12 -0800 From: mmconn[ AT ]silibone.cchem.berkeley.edu (morgan conn) Message-Id: <9511291829.AA15628:~at~:silibone.cchem.berkeley.edu> To: chemistry.,at,.www.ccl.net Subject: binding pocket? Hello all; I'm looking for the impossible. If I have an inhibitor and a protein that are known to associate, and a set of mutations that appear to reduce the in vivo effects of this small molecule, is there a way to (reasonably) find a binding pocket for this molecule on the protein surface? The normal substrate for the molecule shows little, if any, structural similarity to the inhibitor, so the the substrate pocket would _not_ seem to be the binding site. Does anyone have experience/knowledge of this sort of thing. -morgan ******************************************************************** Dr. M. Morgan Conn Department of Chemistry (Schultz group), UC Berkeley mmconn[ AT ]silibone.cchem.berkeley.edu 510.642.9249; 510.643.6890 (fax) ********************************************************************