Crystal structure of ERK2 in complex with (S)-N-(1-(3-chloro-4-fluorophenyl)-2-hydroxyethyl)-4-(4-(3-chlorophenyl)-1H-pyrazol-3-yl)-1H-pyrrole-2-carboxamide
The structure was published by Aronov, A.M., Baker, C., Bemis, G.W., et al., Straub, J., Tang, Q., and Xie, X., in 2007 in a paper entitled "Flipped Out: Structure-Guided Design of Selective Pyrazolylpyrrole ERK Inhibitors." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2007.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Mitogen-activated protein kinase 1. This molecule has the UniProt identifier P28482 (MK01_HUMAN). The sample contained 380 residues which is 100% of the natural sequence. Out of 380 residues 344 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: