ephB4 kinase domain inhibitor complex. Determined by X-ray diffraction at 2.11 Å resolution. Released 23 Oct 2013.
Explore 2YN8 in 3D Show helices and sheets RCSB PDB PDBe
2YN8 contains 32 α-helices and 24 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 609 | 1 | 1 |
| α-helix | 612-614 | 3 | |
| β-strand | 615-623 | 9 | 1 |
| β-strand | 628-634 | 7 | 1 |
| β-strand | 642-649 | 8 | 1 |
| α-helix | 655-669 | 15 | |
| β-strand | 676 | 1 | 2 |
| β-strand | 679-683 | 5 | 1 |
| β-strand | 689-694 | 6 | 1 |
| β-strand | 699-700 | 2 | 2 |
| α-helix | 701-707 | 7 | |
| α-helix | 714-733 | 20 | |
| α-helix | 743-745 | 3 | |
| β-strand | 746-748 | 3 | 2 |
| β-strand | 754-756 | 3 | 2 |
| α-helix | 784-786 | 3 | |
| α-helix | 789-794 | 6 | |
| α-helix | 799-814 | 16 | |
| α-helix | 818-819 | 2 | |
| α-helix | 826-834 | 9 | |
| α-helix | 839-842 | 4 | |
| β-strand | 846 | 1 | 3 |
| α-helix | 847-856 | 10 | |
| α-helix | 861-863 | 3 | |
| α-helix | 865-866 | 2 | |
| α-helix | 867-879 | 13 | |
| α-helix | 881-885 | 5 | |
| β-strand | 887 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ephrin type-B receptor 4 | A, B | protein | 298 | HOMO SAPIENS | P54760 (AlphaFold model) |
>2YN8_1 EPHRIN TYPE-B RECEPTOR 4 (chains A, B) GSSDPNEAVREFAKEIDVSYVKIEEVIGAGEFGEVCRGRLKAPGKKESCVAIKTLKGGYT ERQRREFLSEASIMGQFEHPNIIRLEGVVTNSMPVMILTEFMENGALDSFLRLNDGQFTV IQLVGMLRGIASGMRYLAEMSYVHRDLAARNILVNSNLVCKVSDFGLSRFLEENSSDPTE TSSLGGKIPIRWTAPEAIAFRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIE QDYRLPPPPDCPTSLHQLMLDCWQKDRNARPRFPQIVSALDKMIRNPASLKIVARENG
| ID | Name | Formula | Copies |
|---|---|---|---|
| STU | Staurosporine | C28 H26 N4 O3 | 2 |
Stability and Solubility Engineering of the Ephb4 Tyrosine Kinase Catalytic Domain Using a Rationally Designed Synthetic Library. Overman, R.C., Green, I., Truman, C.M. et al. Protein Eng Des Sel (2013) 26:695. DOI 10.1093/PROTEIN/GZT032 · PubMed
Other PDB entries of the same protein (UniProt P54760 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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