Crystal structure of death associated protein kinase in complex with ADP and Mg2+
The structure was published by McNamara, L.K., Watterson, D.M., and Brunzelle, J.S., in 2009 in a paper entitled "Structural insight into nucleotide recognition by human death-associated protein kinase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.85 Å and deposited in 2008.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Death-associated protein kinase 1. This molecule has the UniProt identifier P53355 (DAPK1_HUMAN). The sample contained 294 residues which is < 90% of the natural sequence. Out of 294 residues 278 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: