Insight to structural subsite recognition in plant thiol protease-inhibitor complexes : Understanding the basis of differential inhibition and the role of water

Table IV (C) Water involved in the interaction inside active site cleft of the enzyme-inhibitor complexes

*Papain + ZPACK*[30]		Distances in Å	Subsites of inhibitor
			in interaction
(No water mediated interaction
was reported)
Caricain + ZPACK
ZPACK:O13	981:OH2	3.01	P3
ZPACK:O3	396:OH2	3.40	P1
ZPACK:O3	402:OH2	2.25^**	P1
Chymopapain + ZPACK
ZPACK:O13	341:OH2	3.14	P3
ZPACK:O14	377:OH2	3.07	P3
ZPACK:N11	377:OH2	3.42'	P2
ZPACK:O3	290:OH2	3.28^**	P1
Actinidin + ZPACK
ZPACK:O13	345:O1	2.84	P3
ZPACK:N6	345:OH2	2.47	P1
ZPACK:O3	366:OH2	2.82^**	P1
Calotropin DI + ZPACK
ZPACK:O13	1279:OH2	3.20	P3
ZPACK:O13	1346:OH2	3.31	P3
ZPACK:O3	1300:OH2	3.09	P1

Foot notes: Names in Italics are x-ray structures Names in normal font are modelled structures ^* denotes the interactions found both in x-ray and modeled structure ^** denotes water found near oxyanion hole

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