Crystal structure and functional characterization of an Asp49 phospholipase A2 from the bushmaster (Lachesis muta)

Neyra Chama, N.E.; Romero Vargas, F.F.; Condori Mamani, E.; Vargas, J.A.; Alves Furtado, A.; D'Muniz Pereira, H.; Navarro Oviedo, R.D.; Garratt, R.C.; Vega Ramírez, J.L.J.; Leonardo, D.A.

doi:10.1107/S2053230X26002736

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
Crystal structure of the Asp49-PLA₂ from L. muta. (a) Overall view of the asymmetric unit showing two independent molecules: chain A and chain B. (b) Close-up of chain A highlighting the Ca²⁺-binding loop and the active site. The inset displays the catalytic dyad formed by His47 and Asp48, the bound Ca²⁺ ion (green sphere) and a MES molecule from the crystallization condition, shown with its polder map (blue mesh) contoured at 2σ. The MES occupies a position within the active-site cleft and interacts with key residues, mimicking substrate recognition.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 82| Part 5| May 2026| Pages 150-159

https://doi.org/10.1107/S2053230X26002736

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