STRUCTURE-BASED DESIGN OF NOVEL CHK1 INHIBITORS: INSIGHTS INTO HYDROGEN BONDING AND PROTEIN-LIGAND AFFINITY
The structure was published by Foloppe, N., Fisher, L.M., Howes, R., et al., Potter, A., Robertson, A.G.S., and Surgenor, A.E., in 2005 in a paper entitled "Structure-Based Design of Novel Chk1 Inhibitors: Insights Into Hydrogen Bonding and Protein-Ligand Affinity." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2005.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of SERINE/THREONINE-PROTEIN KINASE CHK1. This molecule has the UniProt identifier O14757 (CHK1_HUMAN). The sample contained 297 residues which is < 90% of the natural sequence. Out of 297 residues 256 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: