USE OF PAPAIN AS A MODEL FOR THE STRUCTURE-BASED DESIGN OF CATHEPSIN K INHIBITORS. CRYSTAL STRUCTURES OF TWO PAPAIN INHIBITOR COMPLEXES DEMONSTRATE BINDING TO S'-SUBSITES.
The structure was published by LaLonde, J.M., Zhao, B., Smith, W.W., et al., Yamashita, D.S., Veber, D.F., and Abdel-Meguid, S.S., in 1998 in a paper entitled "Use of papain as a model for the structure-based design of cathepsin K inhibitors: crystal structures of two papain-inhibitor complexes demonstrate binding to S'-subsites." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1998.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of PAPAIN. This molecule has the UniProt identifier P00784 (PAPA1_CARPA). The sample contained 212 residues which is < 90% of the natural sequence. Out of 212 residues 212 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: