1khq: Difference between revisions

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[[Image:1khq.~~gif~~|left|200px]]

[[Image:1khq.png|left|200px]]

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~~'''~~ORTHORHOMBIC FORM OF PAPAIN/ZLFG-DAM COVALENT COMPLEX~~'''~~

===ORTHORHOMBIC FORM OF PAPAIN/ZLFG-DAM COVALENT COMPLEX===

~~==Overview==~~

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~~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 line below this paragraph, {{ABSTRACT_PUBMED_15357669}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15357669 is the PubMed ID number.

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==About this Structure==

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[[Category: Irreversible inhibitor]]

[[Category: Protease inhibitor]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 22:45:45 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:21:48 2008''

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-[[Image:1khq.gif|left|200px]]
+{{Seed}}
+[[Image:1khq.png|left|200px]]
 <!--
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 {{STRUCTURE_1khq|  PDB=1khq  |  SCENE=  }}
-'''ORTHORHOMBIC FORM OF PAPAIN/ZLFG-DAM COVALENT COMPLEX'''
+===ORTHORHOMBIC FORM OF PAPAIN/ZLFG-DAM COVALENT COMPLEX===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_15357669}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15357669 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15357669}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Irreversible inhibitor]]
 [[Category: Protease inhibitor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:45:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:21:48 2008''