Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with ANP. Determined by X-ray diffraction at 1.36 Å resolution. Released 9 Nov 2016.
Explore 5I9W in 3D Show helices and sheets RCSB PDB PDBe
5I9W contains 17 α-helices and 12 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 607 | 1 | 1 |
| α-helix | 610-612 | 3 | |
| β-strand | 613-622 | 10 | 1 |
| β-strand | 625-632 | 8 | 1 |
| β-strand | 641-648 | 8 | 1 |
| α-helix | 654-668 | 15 | |
| β-strand | 675 | 1 | 2 |
| β-strand | 678-682 | 5 | 1 |
| β-strand | 688-693 | 6 | 1 |
| β-strand | 699 | 1 | 2 |
| α-helix | 700-706 | 7 | |
| α-helix | 713-732 | 20 | |
| α-helix | 742-744 | 3 | |
| β-strand | 745-747 | 3 | 2 |
| β-strand | 753-755 | 3 | 2 |
| α-helix | 781-783 | 3 | |
| α-helix | 786-791 | 6 | |
| α-helix | 796-811 | 16 | |
| α-helix | 815-816 | 2 | |
| α-helix | 823-832 | 10 | |
| α-helix | 836-839 | 4 | |
| β-strand | 843 | 1 | 3 |
| α-helix | 844-853 | 10 | |
| α-helix | 858-860 | 3 | |
| α-helix | 862-863 | 2 | |
| α-helix | 864-876 | 13 | |
| α-helix | 878-882 | 5 | |
| β-strand | 884 | 1 | 3 |
| α-helix | 885-887 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ephrin type-A receptor 2 | A | protein | 306 | Homo sapiens | P29317 (AlphaFold model) |
>5I9W_1 Ephrin type-A receptor 2 (chains A) GDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTE KQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVL QLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTT SGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGF RLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIR LPSTSG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
Water and common crystallization additives (EDO) are not listed.
Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs. Heinzlmeir, S., Kudlinzki, D., Sreeramulu, S. et al. ACS Chem Biol (2016) 11:3400-3411. DOI 10.1021/acschembio.6b00709 · PubMed
Other PDB entries of the same protein (UniProt P29317 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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