3FZP: PYK2

Crystal structure of PYK2 complexed with ATPgS. Determined by X-ray diffraction at 2.1 Å resolution. Released 31 Mar 2009.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,244
Mol. weight: 32.91 kDa
Ligands: AGS
Released: 31 Mar 2009

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

Secondary structure: helices and β-sheets

3FZP contains 18 α-helices and 9 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: 18 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	422-424	3
β-strand	425-434	10	1
β-strand	437-445	9	1
β-strand	451-458	8	1
α-helix	464-480	17
β-strand	486	1	2
α-helix	487-488	2
β-strand	489-493	5	1
α-helix	498	1
β-strand	499-503	5	1
β-strand	509	1	2
α-helix	510-516	7
α-helix	523-542	20
α-helix	552-554	3
β-strand	555-559	5	2
β-strand	562-565	4	2
α-helix	589-591	3
α-helix	594-599	6
α-helix	604-619	16
α-helix	623-624	2
α-helix	631-633	3
α-helix	634-639	6
α-helix	644-647	4
α-helix	652-661	10
α-helix	666-668	3
α-helix	670-671	2
α-helix	672-691	20

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

>3FZP_1 Protein tyrosine kinase 2 beta (chains A)
PQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEA
VIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICK
AMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPE
SINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPDLCPPVLY
TLMTRCWDYDPSDRPRFTELVCSLSDVYQMEKDIAME

Ligands and cofactors

ID	Name	Formula	Copies
AGS	Phosphothiophosphoric acid-adenylate ester	C10 H16 N5 O12 P3 S	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structural characterization of proline-rich tyrosine kinase 2 (PYK2) reveals a unique (DFG-out) conformation and enables inhibitor design. Han, S., Mistry, A., Chang, J.S. et al. J Biol Chem (2009) 284:13193-13201. DOI 10.1074/jbc.M809038200 · 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
5TOB 2.12 Å, Selectivity switch between FAK and Pyk2: Macrocyclization of FAK inhibitors improves…

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