Crystal structure of a papain-fold protein without the catalytic cysteine from seeds of Pachyrhizus erosus
The structure was published by Zhang, M., Wei, Z., Chang, S., Teng, M., and Gong, W., in 2006 in a paper entitled "Crystal structure of a papain-fold protein without the catalytic residue: a novel member in the cysteine proteinase family" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2005.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely SPE31 and peptide (LYS)(ALA)(SER)(VAL)(GLY).
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 most likely forms heterodimers.
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: