5TO8: Protein-tyrosine kinase 2-beta

Selectivity switch between FAK and Pyk2: Macrocyclization of FAK inhibitors improves Pyk2 potency. Determined by X-ray diffraction at 1.98 Å resolution. Released 21 Dec 2016.

Method: X-ray diffraction
Resolution: 1.98 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,049
Mol. weight: 33.14 kDa
Ligands: 7FM
Released: 21 Dec 2016

Explore 5TO8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5TO8 contains 16 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: 16 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	422-424	3
β-strand	425-433	9	1
β-strand	438-445	8	1
β-strand	451-457	7	1
α-helix	468-480	13
β-strand	486	1	2
α-helix	487-488	2
β-strand	489-493	5	1
β-strand	499-503	5	1
α-helix	504	1
β-strand	509	1	2
α-helix	510-516	7
α-helix	523-541	19
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	594-599	6
α-helix	604-619	16
α-helix	623-624	2
α-helix	631-639	9
α-helix	644-647	4
α-helix	652-661	10
α-helix	666-668	3
α-helix	670-671	2
α-helix	672-690	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein-tyrosine kinase 2-beta	A	protein	282	Homo sapiens	Q14289 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5TO8_1 Protein-tyrosine kinase 2-beta (chains A)
GSMGGPQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEK
FMSEAVIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYS
LQICKAMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIK
WMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPDLC
PPVLYTLMTRCWDYDPSDRPRFTELVCSLSDVYQMEKDIAME

Ligands and cofactors

ID	Name	Formula	Copies
7FM	25-(methylsulfonyl)-8-(trifluoromethyl)-5,17,18,21,22,23,24,25-octahydro-12H-7,…	C25 H26 F3 N7 O3 S	1

Primary citation

Selectivity switch between FAK and Pyk2: Macrocyclization of FAK inhibitors improves Pyk2 potency. Farand, J., Mai, N., Chandrasekhar, J. et al. Bioorg Med Chem Lett (2016) 26:5926-5930. DOI 10.1016/j.bmcl.2016.10.092 · 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
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
5TOB 2.12 Å, Selectivity switch between FAK and Pyk2: Macrocyclization of FAK inhibitors improves…

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