Sandbox Reserved 1105: Difference between revisions

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The central <scene name='82/829358/Hbp2/2'>HBP2</scene> and <scene name='82/829358/Hbp2prime/1'>HBP2'</scene> are formed by the side chains of <scene name='82/829358/Hbp2aa/1'>Leu 110, Ala 109, Lys 15, and Leu 17</scene>, it is primarily hydrophobic with polar or electrostatic contributions from the carbonyl groups of Lys 15, Ala 108 and Ala 109.

The innermost binding ~~pocket~~, HBP3, is located between the side chains of Ser 117, Thr 119, Ala 108 and Leu 110. ~~Its surface is~~ composed of aliphatic methyl and methylene groups, as well as the Ser 117 hydroxyl group, the carbonyl groups of Ser 117, Thr 118 and Ala 108, and the main chain NH groups of Thr 119, Ala 109 and Leu 110.

The innermost binding pockets, <scene name='82/829358/Hbp3/3'>HBP3</scene> and <scene name='82/829358/Hbp3prim/2'>HBP3'</scene>, are located between the side chains of <scene name='82/829358/Hbp3aa/2'>Ser 117, Thr 119, Ala 108 and Leu 110</scene>. Their surfaces are composed of aliphatic methyl and methylene groups, as well as the Ser 117 hydroxyl group, the carbonyl groups of Ser 117, Thr 118 and Ala 108, and the main chain NH groups of Thr 119, Ala 109 and Leu 110.

Sandbox Reserved 1105: Difference between revisions

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Revision as of 19:42, 15 January 2020 view source Léa Wick (talk \| contribs) 61 edits No edit summary ← Older edit		Revision as of 19:54, 15 January 2020 view source Léa Wick (talk \| contribs) 61 edits No edit summary Newer edit →
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	The central <scene name='82/829358/Hbp2/2'>HBP2</scene> and <scene name='82/829358/Hbp2prime/1'>HBP2'</scene> are formed by the side chains of <scene name='82/829358/Hbp2aa/1'>Leu 110, Ala 109, Lys 15, and Leu 17</scene>, it is primarily hydrophobic with polar or electrostatic contributions from the carbonyl groups of Lys 15, Ala 108 and Ala 109.		The central <scene name='82/829358/Hbp2/2'>HBP2</scene> and <scene name='82/829358/Hbp2prime/1'>HBP2'</scene> are formed by the side chains of <scene name='82/829358/Hbp2aa/1'>Leu 110, Ala 109, Lys 15, and Leu 17</scene>, it is primarily hydrophobic with polar or electrostatic contributions from the carbonyl groups of Lys 15, Ala 108 and Ala 109.

	The innermost binding ~~pocket~~, HBP3, is located between the side chains of Ser 117, Thr 119, Ala 108 and Leu 110. ~~Its surface is~~ composed of aliphatic methyl and methylene groups, as well as the Ser 117 hydroxyl group, the carbonyl groups of Ser 117, Thr 118 and Ala 108, and the main chain NH groups of Thr 119, Ala 109 and Leu 110.		The innermost binding pockets, <scene name='82/829358/Hbp3/3'>HBP3</scene> and <scene name='82/829358/Hbp3prim/2'>HBP3'</scene>, are located between the side chains of <scene name='82/829358/Hbp3aa/2'>Ser 117, Thr 119, Ala 108 and Leu 110</scene>. Their surfaces are composed of aliphatic methyl and methylene groups, as well as the Ser 117 hydroxyl group, the carbonyl groups of Ser 117, Thr 118 and Ala 108, and the main chain NH groups of Thr 119, Ala 109 and Leu 110.