Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution.

@article{Frigerio1992CrystalAM,
  title={Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution.},
  author={Franco Frigerio and Alessandro Coda and Luisa Pugliese and Claudia Lionetti and Enea Menegatti and Gino Amiconi and Hans Peter Schnebli and Paolo Ascenzi and Martino Bolognesi},
  journal={Journal of molecular biology},
  year={1992},
  volume={225 1},
  pages={107-23}
}
The crystal structure of the complex between bovine alpha-chymotrypsin and the leech (Hirudo medicinalis) protein proteinase inhibitor eglin c has been refined at 2.0 A resolution to a crystallographic R-factor of 0.167. The structure of the complex includes 2290 protein and 143 solvent atoms. Eglin c is bound to the cognate enzyme through interactions involving 11 residues of the inhibitor (sites P5-P4' in the reactive site loop, P10' and P23') and 17 residues from chymotrypsin. Binding of… CONTINUE READING

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