Crystal structure of MEK1 in complex with fragment 3
The structure was published by Amaning, K., Lowinski, M., Vallee, F., et al., Llopart, S., Halland, N., and Rak, A., in 2013 in a paper entitled "The Use of Virtual Screening and Differential Scanning Fluorimetry for the Rapid Identification of Fragments Active Against Mek1." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.12 Å and deposited in 2013.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 1 MAPK/ERK KINASE 1, MEK 1, MEK1. This molecule has the UniProt identifier Q02750 (MP2K1_HUMAN). The sample contained 348 residues which is < 90% of the natural sequence. Out of 348 residues 309 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: