1khq: Difference between revisions

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[[Image:1khq.gif|left|200px]]<br /><applet load="1khq" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1khq.gif|left|200px]]<br /><applet load="1khq" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1khq, resolution 1.6Å" />

'''ORTHORHOMBIC FORM OF PAPAIN/ZLFG-DAM COVALENT COMPLEX'''<br />

==Overview==

The three-dimensional structure of two polymorphs of a ZLFG-CH2-papain, covalent complex has been determined by X-ray crystallography. The, structures indicate that: (i) the methylene carbon atom of the inhibitor, is covalently bound to the Sgamma atom of Cys25 of papain; (ii) the, hydrophobic S2 pocket formed by Pro68, Val133, Val157, and Asp158 is, occupied by the inhibitor's phenylalanyl P2 side chain; (iii) extensive, hydrogen bonding and hydrophobic interactions are responsible for the, interaction of the inhibitor with the enzyme. Comparison with similar, structures suggests that in covalent complexes preservation of main, chain-main chain interactions between the enzyme and the inhibitor may, have higher priority than the P-S interactions.

The three-dimensional structure of two polymorphs of a ZLFG-CH2-papain covalent complex has been determined by X-ray crystallography. The structures indicate that: (i) the methylene carbon atom of the inhibitor is covalently bound to the Sgamma atom of Cys25 of papain; (ii) the hydrophobic S2 pocket formed by Pro68, Val133, Val157, and Asp158 is occupied by the inhibitor's phenylalanyl P2 side chain; (iii) extensive hydrogen bonding and hydrophobic interactions are responsible for the interaction of the inhibitor with the enzyme. Comparison with similar structures suggests that in covalent complexes preservation of main chain-main chain interactions between the enzyme and the inhibitor may have higher priority than the P-S interactions.

==About this Structure==

1KHQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Carica_papaya Carica papaya]. Active as [http://en.wikipedia.org/wiki/Papain Papain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.2 3.4.22.2] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1KHQ OCA].

1KHQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Carica_papaya Carica papaya]. Active as [http://en.wikipedia.org/wiki/Papain Papain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.2 3.4.22.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KHQ OCA].

==Reference==

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[[Category: protease inhibitor]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 19~~:14:~~50 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:18 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1khq.gif|left|200px]]<br /><applet load="1khq" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1khq.gif|left|200px]]<br /><applet load="1khq" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1khq, resolution 1.6&Aring;" />
 '''ORTHORHOMBIC FORM OF PAPAIN/ZLFG-DAM COVALENT COMPLEX'''<br />
 ==Overview==
-The three-dimensional structure of two polymorphs of a ZLFG-CH2-papain, covalent complex has been determined by X-ray crystallography. The, structures indicate that: (i) the methylene carbon atom of the inhibitor, is covalently bound to the Sgamma atom of Cys25 of papain; (ii) the, hydrophobic S2 pocket formed by Pro68, Val133, Val157, and Asp158 is, occupied by the inhibitor's phenylalanyl P2 side chain; (iii) extensive, hydrogen bonding and hydrophobic interactions are responsible for the, interaction of the inhibitor with the enzyme. Comparison with similar, structures suggests that in covalent complexes preservation of main, chain-main chain interactions between the enzyme and the inhibitor may, have higher priority than the P-S interactions.
+The three-dimensional structure of two polymorphs of a ZLFG-CH2-papain covalent complex has been determined by X-ray crystallography. The structures indicate that: (i) the methylene carbon atom of the inhibitor is covalently bound to the Sgamma atom of Cys25 of papain; (ii) the hydrophobic S2 pocket formed by Pro68, Val133, Val157, and Asp158 is occupied by the inhibitor's phenylalanyl P2 side chain; (iii) extensive hydrogen bonding and hydrophobic interactions are responsible for the interaction of the inhibitor with the enzyme. Comparison with similar structures suggests that in covalent complexes preservation of main chain-main chain interactions between the enzyme and the inhibitor may have higher priority than the P-S interactions.
 ==About this Structure==
-KHQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Carica_papaya Carica papaya]. Active as [http://en.wikipedia.org/wiki/Papain Papain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.2 3.4.22.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KHQ OCA].
+KHQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Carica_papaya Carica papaya]. Active as [http://en.wikipedia.org/wiki/Papain Papain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.2 3.4.22.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KHQ OCA].
 ==Reference==
@@ Line 23: / Line 23: @@
 [[Category: protease inhibitor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:14:50 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:18 2008''