Crystal structure of the EGFR kinase domain mutant V924R. Determined by X-ray diffraction at 1.55 Å resolution. Released 29 Jul 2015.
Explore 5CNO in 3D Show helices and sheets RCSB PDB PDBe
5CNO contains 52 α-helices and 27 β-strands across 3 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 | 677-679 | 3 | |
| β-strand | 681-682 | 2 | 1 |
| α-helix | 683-684 | 2 | |
| α-helix | 685-687 | 3 | |
| β-strand | 688-696 | 9 | 1 |
| β-strand | 700-707 | 8 | 1 |
| β-strand | 716-723 | 8 | 1 |
| α-helix | 724 | 1 | |
| α-helix | 732-743 | 12 | |
| β-strand | 747 | 1 | 2 |
| β-strand | 750 | 1 | 2 |
| α-helix | 751-753 | 3 | |
| β-strand | 755-758 | 4 | 1 |
| β-strand | 762-766 | 5 | 1 |
| β-strand | 773 | 1 | 2 |
| α-helix | 774-780 | 7 | |
| α-helix | 787-806 | 20 | |
| α-helix | 816-818 | 3 | |
| β-strand | 819-823 | 5 | 2 |
| β-strand | 826-829 | 4 | 2 |
| α-helix | 834-838 | 5 | |
| α-helix | 854-856 | 3 | |
| α-helix | 859-864 | 6 | |
| α-helix | 869-884 | 16 | |
| α-helix | 888-889 | 2 | |
| α-helix | 896-898 | 3 | |
| α-helix | 899-904 | 6 | |
| α-helix | 909-912 | 4 | |
| β-strand | 915 | 1 | 3 |
| α-helix | 917-926 | 10 | |
| α-helix | 931-933 | 3 | |
| α-helix | 935-936 | 2 | |
| α-helix | 937-949 | 13 | |
| α-helix | 951-954 | 4 | |
| β-strand | 955 | 1 | 3 |
| α-helix | 960-962 | 3 | |
| α-helix | 964-967 | 4 | |
| α-helix | 968-978 | 11 | |
| α-helix | 984-989 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 677-679 | 3 | |
| β-strand | 681-682 | 2 | 4 |
| α-helix | 685-687 | 3 | |
| β-strand | 688-696 | 9 | 4 |
| β-strand | 700-707 | 8 | 4 |
| β-strand | 716-723 | 8 | 4 |
| α-helix | 732-743 | 12 | |
| β-strand | 747 | 1 | 5 |
| β-strand | 750 | 1 | 5 |
| α-helix | 751-753 | 3 | |
| β-strand | 755-758 | 4 | 4 |
| β-strand | 762-766 | 5 | 4 |
| β-strand | 773 | 1 | 5 |
| α-helix | 774-780 | 7 | |
| α-helix | 787-806 | 20 | |
| α-helix | 816-818 | 3 | |
| β-strand | 819-823 | 5 | 5 |
| β-strand | 826-829 | 4 | 5 |
| α-helix | 834-837 | 4 | |
| α-helix | 854-856 | 3 | |
| α-helix | 859-864 | 6 | |
| α-helix | 869-884 | 16 | |
| α-helix | 888-889 | 2 | |
| α-helix | 896-898 | 3 | |
| α-helix | 899-904 | 6 | |
| α-helix | 909-912 | 4 | |
| β-strand | 915 | 1 | 6 |
| α-helix | 917-926 | 10 | |
| α-helix | 931-933 | 3 | |
| α-helix | 935-936 | 2 | |
| α-helix | 937-948 | 12 | |
| α-helix | 951-954 | 4 | |
| β-strand | 955 | 1 | 6 |
| α-helix | 960-962 | 3 | |
| α-helix | 964-967 | 4 | |
| α-helix | 968-978 | 11 | |
| α-helix | 984-989 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 995 | 1 | |
| β-strand | 996 | 1 | 4 |
| α-helix | 997 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Epidermal growth factor receptor | A, B, X | protein | 330 | Homo sapiens | P00533 (AlphaFold model) |
>5CNO_1 Epidermal growth factor receptor (chains A, B, X) GAMGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATS PKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQ YLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAE GGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGER LPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSP TDSNFYRALMDEEDMDDVVDADEYLIPQQG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
| MG | Magnesium ion | Mg | 2 |
Analysis of the Role of the C-Terminal Tail in the Regulation of the Epidermal Growth Factor Receptor. Kovacs, E., Das, R., Wang, Q. et al. Mol Cell Biol (2015) 35:3083-3102. DOI 10.1128/MCB.00248-15 · 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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