3PA4: Compound 2a

X-ray crystal structure of compound 2a bound to human CHK1 kinase domain. Determined by X-ray diffraction at 1.59 Å resolution. Released 8 Dec 2010.

Method: X-ray diffraction
Resolution: 1.59 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,403
Mol. weight: 32.12 kDa
Ligands: C72
Released: 8 Dec 2010

Explore 3PA4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3PA4 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	9-16	8	1
β-strand	22-28	7	1
β-strand	34-40	7	1
α-helix	52-59	8
β-strand	67	1	2
α-helix	68-69	2
β-strand	70-75	6	1
β-strand	80-85	6	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

>3PA4_1 Serine/threonine-protein kinase Chk1 (chains A)
AVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINKM
LNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVYL
HGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLKR
REFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLAL
LHKILVENPSARITIPDIKKDRWYNKPLKKGAK

Ligands and cofactors

ID	Name	Formula	Copies
C72	2-(4-chlorophenyl)-4-[(3S)-piperidin-3-ylamino]thieno[3,2-c]pyridine-7-carboxam…	C19 H19 Cl N4 O S	1

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

Primary citation

Design, synthesis and SAR of thienopyridines as potent CHK1 inhibitors. Zhao, L., Zhang, Y., Dai, C. et al. Bioorg Med Chem Lett (2010) 20:7216-7221. DOI 10.1016/j.bmcl.2010.10.105 · 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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