Journal:Acta Cryst F:S2053230X21008761
From Proteopedia
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<scene name='89/890854/Cv/9'>The interface interactions between VinK and VinL</scene> are essentially the same between these two VinK-VinL complex structures, suggesting that interface interactions are not affected by the cross-linking strategy used. This structural observation expands our understanding of the structure-function relationships of acyltransferases. Salt bridges are shown as dashed lines, helix II is colored in deep sky blue. | <scene name='89/890854/Cv/9'>The interface interactions between VinK and VinL</scene> are essentially the same between these two VinK-VinL complex structures, suggesting that interface interactions are not affected by the cross-linking strategy used. This structural observation expands our understanding of the structure-function relationships of acyltransferases. Salt bridges are shown as dashed lines, helix II is colored in deep sky blue. | ||
| - | PDB reference: VinK–VinL covalent complex with a pantetheineamide cross-linking probe, [[7f2r]]. | + | '''PDB reference:''' VinK–VinL covalent complex with a pantetheineamide cross-linking probe, [[7f2r]]. |
<b>References</b><br> | <b>References</b><br> | ||
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