X-RAY CRYSTALLOGRAPHIC STRUCTURE OF A PAPAIN-LEUPEPTIN COMPLEX

File:1pop.gif


1pop, resolution 2.1Å

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OverviewOverview

The three-dimensional structure of the papain-leupeptin complex has been determined by X-ray crystallography to a resolution of 2.1 A (overall R-factor = 19.8%). The structure indicates that: (i) leupeptin contacts the S subsites of the papain active site and not the S' subsites; (ii) the 'carbonyl' carbon atom of the inhibitor is covalently bound by the Cys-25 sulphur atom of papain and is tetrahedrally coordinated; (iii) the 'carbonyl' oxygen atom of the inhibitor faces the oxyanion hole and makes hydrogen bond contacts with Gln-19 and Cys-25.

About this StructureAbout this Structure

1POP is a Single protein structure of sequence from [1] with and as ligands. Active as Papain, with EC number 3.4.22.2 Full crystallographic information is available from OCA.

ReferenceReference

X-ray crystallographic structure of a papain-leupeptin complex., Schroder E, Phillips C, Garman E, Harlos K, Crawford C, FEBS Lett. 1993 Jan 2;315(1):38-42. PMID:8416808

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