Crystal Structure of EGFR T790M/V948R in Complex with Covalent Pyrrolopyrimidine 21a. Determined by X-ray diffraction at 1.5 Å resolution. Released 30 Sept 2020.
Explore 6TG0 in 3D Show helices and sheets RCSB PDB PDBe
6TG0 contains 41 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 |
|---|---|---|---|
| α-helix | 701-703 | 3 | |
| β-strand | 705-706 | 2 | 1 |
| α-helix | 709-711 | 3 | |
| β-strand | 712-721 | 10 | 1 |
| β-strand | 724-731 | 8 | 1 |
| β-strand | 740-747 | 8 | 1 |
| α-helix | 748-750 | 3 | |
| α-helix | 756-768 | 13 | |
| β-strand | 774 | 1 | 2 |
| β-strand | 779-782 | 4 | 1 |
| β-strand | 786-791 | 6 | 1 |
| β-strand | 797 | 1 | 2 |
| α-helix | 798-805 | 8 | |
| α-helix | 806-808 | 3 | |
| α-helix | 811-830 | 20 | |
| α-helix | 840-842 | 3 | |
| β-strand | 843-847 | 5 | 2 |
| β-strand | 850-853 | 4 | 2 |
| α-helix | 878-880 | 3 | |
| α-helix | 883-888 | 6 | |
| α-helix | 893-908 | 16 | |
| α-helix | 912-913 | 2 | |
| α-helix | 920-922 | 3 | |
| α-helix | 923-928 | 6 | |
| α-helix | 933-936 | 4 | |
| β-strand | 939 | 1 | 3 |
| α-helix | 941-950 | 10 | |
| α-helix | 955-957 | 3 | |
| α-helix | 959-960 | 2 | |
| α-helix | 961-972 | 12 | |
| α-helix | 975-978 | 4 | |
| β-strand | 979 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 701-703 | 3 | |
| β-strand | 705-706 | 2 | 4 |
| α-helix | 709-711 | 3 | |
| β-strand | 712-720 | 9 | 4 |
| β-strand | 724-731 | 8 | 4 |
| β-strand | 740-747 | 8 | 4 |
| α-helix | 750-751 | 2 | |
| α-helix | 756-768 | 13 | |
| β-strand | 774 | 1 | 5 |
| β-strand | 779-782 | 4 | 4 |
| β-strand | 786-791 | 6 | 4 |
| β-strand | 797 | 1 | 5 |
| α-helix | 798-804 | 7 | |
| α-helix | 806-808 | 3 | |
| α-helix | 811-830 | 20 | |
| α-helix | 840-842 | 3 | |
| β-strand | 843-847 | 5 | 5 |
| β-strand | 850-853 | 4 | 5 |
| α-helix | 857-860 | 4 | |
| α-helix | 878-880 | 3 | |
| α-helix | 883-888 | 6 | |
| α-helix | 893-908 | 16 | |
| α-helix | 912-913 | 2 | |
| α-helix | 920-922 | 3 | |
| α-helix | 923-928 | 6 | |
| α-helix | 933-936 | 4 | |
| β-strand | 939 | 1 | 6 |
| α-helix | 941-950 | 10 | |
| α-helix | 955-957 | 3 | |
| α-helix | 959-960 | 2 | |
| α-helix | 961-971 | 11 | |
| α-helix | 975-978 | 4 | |
| β-strand | 979 | 1 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Epidermal growth factor receptor | A, B | protein | 333 | Homo sapiens | P00533 (AlphaFold model) |
>6TG0_1 Epidermal growth factor receptor (chains A, B) GSHMASGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELRE ATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGCLLDYVREHKDNI GSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEY HAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEK GERLPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHL PSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG
| ID | Name | Formula | Copies |
|---|---|---|---|
| N78 | ~{N}-[5-[4-[[4-[[1,3-bis(oxidanylidene)isoindol-2-yl]methyl]phenyl]amino]-7~{H}… | C32 H28 N6 O5 | 2 |
Water and common crystallization additives (EDO, SO4) are not listed.
Targeting Her2-insYVMA with Covalent Inhibitors-A Focused Compound Screening and Structure-Based Design Approach. Lategahn, J., Hardick, J., Grabe, T. et al. J Med Chem (2020) 63:11725-11755. DOI 10.1021/acs.jmedchem.0c00870 · PubMed
Other PDB entries of the same protein (UniProt P00533 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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