CRYSTAL STRUCTURE OF HUMAN STE20-LIKE KINASE (DIPHOSPHORYLATED FORM) BOUND TO 5- AMINO-3-((4-(AMINOSULFONYL)PHENYL)AMINO)-N-(2,6- DIFLUOROPHENYL)-1H-1,2, 4-TRIAZOLE-1-CARBOTHIOAMIDE
The structure was published by Pike, A.C.W., Rellos, P., Niesen, F.H., et al., Turk, B.E., Pearl, L.H., and Knapp, S., in 2008 in a paper entitled "Activation Segment Dimerization: A Mechanism for Kinase Autophosphorylation of Non-Consensus Sites." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2007.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of STE20-LIKE SERINE/THREONINE-PROTEIN KINASE.
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 homodimers.
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: