3ET7: PYK2

Crystal structure of PYK2 complexed with PF-2318841. Determined by X-ray diffraction at 2.7 Å resolution. Released 23 Jun 2009.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,168
Mol. weight: 32.82 kDa
Ligands: 349, PO4
Released: 23 Jun 2009

Explore 3ET7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3ET7 contains 15 α-helices and 11 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: 15 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	422-424	3
β-strand	426-432	7	1
β-strand	439-443	5	1
β-strand	453-457	5	1
α-helix	466-480	15
β-strand	486	1	2
β-strand	489-493	5	1
β-strand	499-503	5	1
β-strand	509	1	2
α-helix	512-515	4
α-helix	526-542	17
β-strand	546-547	2	3
α-helix	552-554	3
β-strand	555-559	5	2
β-strand	562-565	4	2
β-strand	570-571	2	3
α-helix	589-591	3
α-helix	594-598	5
α-helix	604-618	15
α-helix	631-633	3
α-helix	634-640	7
α-helix	654-660	7
α-helix	666-668	3
α-helix	670-671	2
α-helix	672-679	8
α-helix	681-684	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein tyrosine kinase 2 beta	A	protein	277	Homo sapiens	Q14289 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3ET7_1 Protein tyrosine kinase 2 beta (chains A)
PQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEA
VIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICK
AMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPE
SINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPDLCPPVLY
TLMTRCWDYDPSDRPRFTELVCSLSDVYQMEKDIAME

Ligands and cofactors

ID	Name	Formula	Copies
349	5-{[4-{[2-(pyrrolidin-1-ylsulfonyl)benzyl]amino}-5-(trifluoromethyl)pyrimidin-2…	C24 H21 F3 N6 O3 S	1
PO4	Phosphate ion	O4 P	1

Primary citation

Trifluoromethylpyrimidine-based inhibitors of proline-rich tyrosine kinase 2 (PYK2): structure-activity relationships and strategies for the elimination of reactive metabolite formation. Walker, D.P., Bi, F.C., Kalgutkar, A.S. et al. Bioorg Med Chem Lett (2008) 18:6071-6077. DOI 10.1016/j.bmcl.2008.10.030 · PubMed

Other PDB entries of the same protein (UniProt Q14289 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3CC6 1.6 Å, Crystal structure of kinase domain of protein tyrosine kinase 2 beta (PTK2B)
3FZS 1.75 Å, Crystal Structure of PYK2 complexed with BIRB796
4XEK 1.79 Å, Pyk2-FAT domain in complex with leupaxin LD4 motif
8XOX 1.9 Å, The Crystal Structure of FAK2 from Biortus.
3FZT 1.95 Å, Crystal structure of PYK2 complexed with PF-4618433
5TO8 1.98 Å, Selectivity switch between FAK and Pyk2: Macrocyclization of FAK inhibitors improves…
4H1M 1.99 Å, Crystal structure of PYK2 with the indole 10c
3H3C 2.0 Å, Crystal structure of PYK2 in complex with Sulfoximine-substituted…
4H1J 2.0 Å, Crystal structure of PYK2 with the pyrazole 13a
8YGX 2.0 Å, Structure of the PYK2 from Biortus.
4XEV 2.01 Å, Fusion of Pyk2-FAT domain with Leupaxin LD1 motif, complexed with Leupaxin LD4 peptide
3FZP 2.1 Å, Crystal structure of PYK2 complexed with ATPgS

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