Crystal structure of plant cysteine protease Ervatamin-C complexed with irreversible inhibitor E-64 at 2.7 A resolution
The structure was published by Ghosh, R., Chakraborty, S., Chakrabarti, C., Dattagupta, J.K., and Biswas, S., in 2008 in a paper entitled "Structural insights into the substrate specificity and activity of ervatamins, the papain-like cysteine proteases from a tropical plant, Ervatamia coronaria." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 2007.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Ervatamin-C.
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 has more than one probable quaternary state observed. For more details see the quaternary structure page.
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: