3U3F: Protein-tyrosine kinase 2-beta
Structural basis for the interaction of Pyk2 PAT domain with paxillin LD motifs. Determined by X-ray diffraction at 3.1 Å resolution. Released 24 Oct 2012.
- Method
- X-ray diffraction
- Resolution
- 3.1 Å
- Organism
- Homo sapiens
- Chains
- 10
- Atoms
- 4,292
- Mol. weight
- 72.53 kDa
- Released
- 24 Oct 2012
Explore 3U3F in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3U3F contains 26 α-helices and 0 β-strands across 10 chains. 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: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 879-895 | 17 | |
| α-helix | 903-905 | 3 | |
| α-helix | 906-927 | 22 | |
| α-helix | 933-962 | 30 | |
| α-helix | 969-1004 | 36 | |
Chain B: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 879-897 | 19 | |
| α-helix | 903-905 | 3 | |
| α-helix | 906-925 | 20 | |
| α-helix | 928-930 | 3 | |
| α-helix | 933-962 | 30 | |
| α-helix | 969-1004 | 36 | |
Chain C: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 879-897 | 19 | |
| α-helix | 903-925 | 23 | |
| α-helix | 928-930 | 3 | |
| α-helix | 933-962 | 30 | |
| α-helix | 969-1001 | 33 | |
Chain D: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 879-897 | 19 | |
| α-helix | 903-927 | 25 | |
| α-helix | 933-962 | 30 | |
| α-helix | 969-1001 | 33 | |
Chains E, F and G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 263-272 | 10 | |
Chain H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 263-273 | 11 | |
Chain I: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 267-273 | 7 | |
Chain J: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 267-274 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein-tyrosine kinase 2-beta | A, B, C, D | protein | 139 | Homo sapiens | Q14289 (AlphaFold model) |
| Paxillin LD2 peptide | E, F, G, H, I, J | protein | 17 | Homo sapiens | P49023 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>3U3F_1 Protein-tyrosine kinase 2-beta (chains A, B, C, D)
GSHMANLDRTDDLVYLNVMELVRAVLELKNELSQLPPEGYVVVVKNVGLTLRKLIGSVDD
LLPSLPSSSRTEIEGTQKLLNKDLAELINKMRLAQQNAVTSLSEECKRQMLTASHTLAVD
AKNLLDAVDQAKVLANLAH
Sequence of entity 2 (E, F, G, H, I, J), FASTA
>3U3F_2 Paxillin LD2 peptide (chains E, F, G, H, I, J)
SATRELDELMASLSDFK
Primary citation
Structural and Mechanistic Insights into the Interaction between Pyk2 and Paxillin LD Motifs. Vanarotti, M.S., Miller, D.J., Guibao, C.D. et al. J Mol Biol (2014) 426:3985-4001. DOI 10.1016/j.jmb.2014.08.014 · 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
Browse structure collections
About this viewer
MolViewer shows 3U3F directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.