EGFR Kinase domain complexed with tak-285. Determined by X-ray diffraction at 1.5 Å resolution. Released 30 Mar 2011.
Explore 3POZ in 3D Show helices and sheets RCSB PDB PDBe
3POZ contains 21 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 |
|---|---|---|---|
| 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 | 740-746 | 7 | 1 |
| α-helix | 756-768 | 13 | |
| β-strand | 771 | 1 | 2 |
| β-strand | 774 | 1 | 2 |
| β-strand | 777-782 | 6 | 1 |
| β-strand | 786-791 | 6 | 1 |
| β-strand | 797 | 1 | 2 |
| α-helix | 798-804 | 7 | |
| α-helix | 811-830 | 20 | |
| α-helix | 840-842 | 3 | |
| β-strand | 843-847 | 5 | 2 |
| β-strand | 850-853 | 4 | 2 |
| α-helix | 858-862 | 5 | |
| 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 | 996-1002 | 7 | |
| α-helix | 1013-1016 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Epidermal growth factor receptor | A | protein | 327 | Homo sapiens | P00533 (AlphaFold model) |
>3POZ_1 Epidermal growth factor receptor (chains A) GEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKA NKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLL NWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGK VPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQ PPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDS NFYRALMDEEDMDDVVDADEYLIPQQG
| ID | Name | Formula | Copies |
|---|---|---|---|
| 03P | N-{2-[4-({3-chloro-4-[3-(trifluoromethyl)phenoxy]phenyl}amino)-5H-pyrrolo[3,2-d… | C26 H25 Cl F3 N5 O3 | 1 |
Water and common crystallization additives (SO4) are not listed.
Structural Analysis of the Mechanism of Inhibition and Allosteric Activation of the Kinase Domain of HER2 Protein. Aertgeerts, K., Skene, R., Yano, J. et al. J Biol Chem (2011) 286:18756-18765. DOI 10.1074/jbc.M110.206193 · 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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