Proposed Amino Acid Sequence and the 1.63 Angstrom X-ray Crystal Structure of a Plant Cysteine Protease Ervatamin B: Insight into the Structural Basis of its Stability and Substrate Specificity.
The structure was published by Biswas, S., Chakrabarti, C., Kundu, S, Jagannadham, M.V., and Dattagupta, J.K., in 2003 in a paper entitled "Proposed amino acid sequence and the 1.63 A X-ray crystal structure of a plant cysteine protease, ervatamin B: Some insights into the structural basis of its stability and substrate specificity" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.63 Å and deposited in 2002.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of ERVATAMIN B. This molecule has the UniProt identifier P60994 (ERVB_TABDI). The sample contained 215 residues which is 100% of the natural sequence. Out of 215 residues 215 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: