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The plots show the ligand's Trp 252 residue nestling in the highly hydrophobic specificity pocket of the enzyme's active site.
Two aspartate residues participate in acid/base catalysis at the active site.
Difference electron density for a molecule of AMPPNP is observed in the kinase active site cleft.
Although the active site of ASV integrase does not undergo significant conformational changes on binding the required metal cofactor, that of HIV-1 does.
Characterisation of a novel methanol dehydrogenase containing a Ba 2+ ion at the active site.
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