Structure-based Design of Novel Chk1 Inhibitors: Insights into Hydrogen Bonding and Protein-Ligand Affinity

N-TERMINAL KINASE DOMAIN, RESIDUES 1-289

MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINKMLNHENVVKFYGHRREGNIQ
YLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNR
ERLLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLA
LLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRPRVTSGGVSESPSGHHHHHHHH

THE 1.7 A CRYSTAL STRUCTURE OF HUMAN CELL CYCLE CHECKPOINTKINASE CHK1

THE COMPLEX STRUCTURE OF CHECKPOINT KINASE CHK1/UCN-01

THE COMPLEX STRUCTURE OF CHECKPOINT KINASE CHK1/STAUROSPORINE

THE COMPLEX STRUCTURE OF CHECKPOINT KINASE CHK1/SB218078

SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.

FUNCTION: PARTICIPATES IN THE ARREST OF THE CELL CYCLE WHEN THE DNA IS DAMAGED OR WHEN UNLIGATED DNA IS PRESENT

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

DRUG DESIGN, FURANOPYRIMIDINE, MOLECULAR RECOGNITION, ONCOLOGY, PYRROLOPYRIMIDINE, ATP-BINDING, CELL CYCLE, DNA DAMAGE, KINASE, NUCLEAR PROTEIN, PHOSPHORYLATION, POLYMORPHISM, SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE