3OT8: Compound 17r

X-ray crystal structure of compound 17r bound to human Chk1 kinase domain. Determined by X-ray diffraction at 1.65 Å resolution. Released 10 Nov 2010.

Method: X-ray diffraction
Resolution: 1.65 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,318
Mol. weight: 32.13 kDa
Ligands: MI5
Released: 10 Nov 2010

Explore 3OT8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3OT8 contains 12 α-helices and 17 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 12 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	9-16	8	1
β-strand	22-28	7	1
β-strand	34-39	6	1
α-helix	52-59	8
β-strand	67	1	2
β-strand	70-73	4	1
β-strand	81-85	5	1
β-strand	90-91	2	2
α-helix	92-95	4
β-strand	97	1	3
β-strand	101	1	3
α-helix	104-123	20
β-strand	126-127	2	4
α-helix	133-135	3
β-strand	136-138	3	2
β-strand	144-146	3	2
β-strand	153-154	2	4
β-strand	156-157	2	5
β-strand	160-161	2	5
β-strand	164	1	6
α-helix	171-173	3
α-helix	176-180	5
β-strand	184	1	6
α-helix	186-203	18
α-helix	216-222	7
α-helix	231-233	3
α-helix	236-245	10
α-helix	254-255	2
α-helix	256-259	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase Chk1	A	protein	273	Homo sapiens	O14757 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3OT8_1 Serine/threonine-protein kinase Chk1 (chains A)
AVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINKM
LNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVYL
HGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLKR
REFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLAL
LHKILVENPSARITIPDIKKDRWYNKPLKKGAK

Ligands and cofactors

ID	Name	Formula	Copies
MI5	N-(3-methylisothiazol-5-yl)-3-(1-methyl-1H-pyrazol-4-yl)-5-[(3R)-piperidin-3-yl…	C19 H22 N8 S	1

Water and common crystallization additives (GOL) are not listed.

Primary citation

Discovery of pyrazolo[1,5-a]pyrimidine-based CHK1 inhibitors: A template-based approach-Part 1. Dwyer, M.P., Paruch, K., Labroli, M. et al. Bioorg Med Chem Lett (2011) 21:467-470. DOI 10.1016/j.bmcl.2010.10.113 · PubMed

Other PDB entries of the same protein (UniProt O14757 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2YEX 1.3 Å, Synthesis and evaluation of triazolones as checkpoint kinase 1 inhibitors
9CE4 1.31 Å, Structure of CHK1 10-pt. mutant complex with LRRK2 indazole inhibitor compound 6
4HYI 1.4 Å, X-RAY Crystal structure of compound 40 bound to human chk1 kinase domain
3PA3 1.4 Å, X-ray crystal structure of compound 70 bound to human CHK1 kinase domain
5OQ5 1.4 Å, Structure of CHK1 8-pt. mutant complex with aminopyrimido-benzodiazepinone LRRK2 inhibitor
3OT3 1.44 Å, X-ray crystal structure of compound 22k bound to human Chk1 kinase domain
7SUF 1.48 Å, Structure of CHK1 10-pt. mutant complex with LRRK2 inhibitor 06
7SUG 1.48 Å, Structure of CHK1 10-pt. mutant complex with LRRK2 inhibitor 09
8E80 1.49 Å, Structure of LRRK2-CHK1 10-pt. mutant complex with heteroaryl-1H-indazole LRRK2…
5OPB 1.55 Å, Structure of CHK1 10-pt. mutant complex with indazole LRRK2 inhibitor
5OPU 1.55 Å, Structure of CHK1 10-pt. mutant complex with pyrrolopyridine LRRK2 inhibitor
8SIX 1.55 Å, Structure of Compound 13 bound to the CHK1 10-point mutant

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