EGFR kinase domain (T790MV948R) in complex with a strain-release covalent inhibitor. Determined by X-ray diffraction at 1.55 Å resolution. Released 29 Jul 2026.
Explore 9NTP in 3D Show helices and sheets RCSB PDB PDBe
9NTP contains 26 α-helices and 13 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 |
|---|---|---|---|
| α-helix | 701-703 | 3 | |
| β-strand | 705-706 | 2 | 1 |
| α-helix | 707-708 | 2 | |
| α-helix | 709-711 | 3 | |
| β-strand | 712-720 | 9 | 1 |
| β-strand | 724-731 | 8 | 1 |
| β-strand | 740-747 | 8 | 1 |
| α-helix | 755-767 | 13 | |
| β-strand | 771 | 1 | 2 |
| β-strand | 774 | 1 | 2 |
| α-helix | 775-777 | 3 | |
| β-strand | 779-782 | 4 | 1 |
| β-strand | 786-790 | 5 | 1 |
| β-strand | 797 | 1 | 2 |
| 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 | 2 |
| β-strand | 850-853 | 4 | 2 |
| α-helix | 858-861 | 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 | 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 |
| α-helix | 984-986 | 3 | |
| α-helix | 989-991 | 3 | |
| α-helix | 992-1002 | 11 | |
| α-helix | 1008-1013 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Epidermal growth factor receptor | A | protein | 329 | Homo sapiens | P00533 (AlphaFold model) |
>9NTP_1 Epidermal growth factor receptor (chains A) GPGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSP KANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGCLLDYVREHKDNIGSQY LLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEG GKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERL PQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPT DSNFYRALMDEEDMDDVVDADEYLIPQQG
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1B6E | N-[4-(3-chloro-4-fluoroanilino)-7-{[(3S)-oxolan-3-yl]oxy}quinazolin-6-yl]cyclob… | C22 H22 Cl F N4 O4 S | 1 |
Water and common crystallization additives (EDO) are not listed.
Late-stage functionalization with strain-release warheads enables tunable covalent inhibition. Shultz, Z.P., Lee-Sam, A., Chang, Y.P. et al. Science (2026) 393:408-416. DOI 10.1126/science.adx7219 · 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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