Probing ligand binding of endothiapepsin by `temperature-resolved' macromolecular crystallography

Huang, C.-Y.; Aumonier, S.; Engilberge, S.; Eris, D.; Smith, K.M.L.; Leonarski, F.; Wojdyla, J.A.; Beale, J.H.; Buntschu, D.; Pauluhn, A.; Sharpe, M.E.; Metz, A.; Olieric, V.; Wang, M.

doi:10.1107/S205979832200612X

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 4
Molecular interactions of TL00150 and EP. Molecular interactions of EP–TL00150 in (a) S1′, (b) both S1′ and S1 and (c) S1 of EP. All relevant hydrogen bonds are depicted as dashed lines. The flap domain, the S1 and S1′ positions of the EP active-site pocket and residues involved in the hydrogen-bonding network are shown. The DMSO and water molecules with a blue shadow are not observed in some RT structures. The residues with a red shadow show an alternative conformation in 100 K structures.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 78| Part 8| August 2022| Pages 964-974

https://doi.org/10.1107/S205979832200612X

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