STRUCTURE OF ONCOMODULIN REFINED AT 1.85 ANGSTROMS RESOLUTION. AN EXAMPLE OF EXTENSIVE MOLECULAR AGGREGATION VIA CA2+
The structure was published by Ahmed, F.R., Przybylska, M., Rose, D.R., Birnbaum, G.I., Pippy, M.E., and MacManus, J.P., in 1990 in a paper entitled "Structure of oncomodulin refined at 1.85 A resolution. An example of extensive molecular aggregation via Ca2+." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.85 Å and deposited in 1990.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of ONCOMODULIN. This molecule has the UniProt identifier P02631 (ONCO_RAT). The sample contained 108 residues which is 99% of the natural sequence. Out of 108 residues 107 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: