8SIX: Compound 13

Structure of Compound 13 bound to the CHK1 10-point mutant. Determined by X-ray diffraction at 1.55 Å resolution. Released 1 Nov 2023.

Method: X-ray diffraction
Resolution: 1.55 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,346
Mol. weight: 34.6 kDa
Ligands: ZXP
Released: 1 Nov 2023

Explore 8SIX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8SIX contains 13 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: 13 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	11-17	7	1
β-strand	22-27	6	1
β-strand	34-41	8	1
α-helix	50-61	12
β-strand	67	1	2
α-helix	68-69	2
β-strand	70-76	7	1
β-strand	79-84	6	1
β-strand	90-91	2	2
α-helix	93-95	3
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	297	Homo sapiens	O14757 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8SIX_1 Serine/threonine-protein kinase Chk1 (chains A)
MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICILK
MLNHENVIKFYGHRREGNIQYLFMELASGGSLFDRIEPDIGMPEPDAQRFFHQLMAGVVY
LHGIGITHRDIKPHNLLLDERDNLKIADYSLATVFRYNNRERLLNKMCGTLPYVAPELLK
RREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLA
LLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRPRVTSGGVSESPSGHHHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
ZXP	(1S)-N-(7-chloro-6-{4-[(3R,4R)-4-hydroxy-3-methyloxolan-3-yl]piperazin-1-yl}iso…	C26 H33 Cl N4 O4	1

Primary citation

Discovery of MK-1468: A Potent, Kinome-Selective, Brain-Penetrant Amidoisoquinoline LRRK2 Inhibitor for the Potential Treatment of Parkinson's Disease. Kattar, S.D., Gulati, A., Margrey, K.A. et al. J Med Chem (2023) 66:14912-14927. DOI 10.1021/acs.jmedchem.3c01486 · 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
3PA4 1.59 Å, X-ray crystal structure of compound 2a bound to human CHK1 kinase domain

Browse structure collections

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