Crystal structure of EGFR kinase domain G719S mutation in complex with Iressa. Determined by X-ray diffraction at 3.25 Å resolution. Released 3 Apr 2007.
Explore 2ITO in 3D Show helices and sheets RCSB PDB PDBe
2ITO contains 20 α-helices and 17 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 | 702-705 | 4 | |
| β-strand | 706 | 1 | 1 |
| α-helix | 707-708 | 2 | |
| α-helix | 709-711 | 3 | |
| β-strand | 714-719 | 6 | 1 |
| β-strand | 724-731 | 8 | 1 |
| β-strand | 739 | 1 | 2 |
| β-strand | 740-747 | 8 | 1 |
| α-helix | 753-768 | 16 | |
| β-strand | 771 | 1 | 3 |
| β-strand | 774 | 1 | 3 |
| β-strand | 777-781 | 5 | 1 |
| β-strand | 787-791 | 5 | 1 |
| β-strand | 797 | 1 | 3 |
| α-helix | 798-804 | 7 | |
| α-helix | 811-830 | 20 | |
| β-strand | 833-834 | 2 | 4 |
| α-helix | 840-842 | 3 | |
| β-strand | 843-847 | 5 | 3 |
| β-strand | 850-853 | 4 | 3 |
| β-strand | 860-861 | 2 | 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 | 923-929 | 7 | |
| α-helix | 933-936 | 4 | |
| β-strand | 939 | 1 | 5 |
| α-helix | 941-949 | 9 | |
| α-helix | 959-960 | 2 | |
| α-helix | 961-971 | 11 | |
| α-helix | 975-977 | 3 | |
| β-strand | 979 | 1 | 5 |
| α-helix | 984-986 | 3 | |
| β-strand | 1010 | 1 | 2 |
| α-helix | 1013-1015 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Epidermal growth factor receptor | A | protein | 327 | HOMO SAPIENS | P00533 (AlphaFold model) |
>2ITO_1 EPIDERMAL GROWTH FACTOR RECEPTOR (chains A) GEAPNQALLRILKETEFKKIKVLSSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKA NKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLL NWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGK VPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQ PPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDS NFYRALMDEEDMDDVVDADEYLIPQQG
| ID | Name | Formula | Copies |
|---|---|---|---|
| IRE | Gefitinib | C22 H24 Cl F N4 O3 | 1 |
Structures of Lung Cancer-Derived Egfr Mutants and Inhibitor Complexes: Mechanism of Activation and Insights Into Differential Inhibitor Sensitivity. Yun, C.-H., Boggon, T.J., Li, Y. et al. Cancer Cell (2007) 11:217. DOI 10.1016/J.CCR.2006.12.017 · PubMed
Other PDB entries of the same protein (UniProt P00533 (AlphaFold model), which also has an AlphaFold model), best resolution first:
2ITO is part of these collections:
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