Crystal Structure of the Kinase domain of Human HER2 (erbB2). Determined by X-ray diffraction at 2.25 Å resolution. Released 30 Mar 2011.
Explore 3PP0 in 3D Show helices and sheets RCSB PDB PDBe
3PP0 contains 41 α-helices and 32 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 |
|---|---|---|---|
| β-strand | 714 | 1 | 1 |
| α-helix | 717-719 | 3 | |
| β-strand | 720-728 | 9 | 1 |
| β-strand | 732-739 | 8 | 1 |
| β-strand | 748-755 | 8 | 1 |
| α-helix | 756 | 1 | |
| α-helix | 761-774 | 14 | |
| β-strand | 782 | 1 | 2 |
| β-strand | 785-790 | 6 | 1 |
| β-strand | 794-799 | 6 | 1 |
| β-strand | 805 | 1 | 2 |
| α-helix | 806-812 | 7 | |
| α-helix | 819-838 | 20 | |
| β-strand | 841-842 | 2 | 3 |
| α-helix | 848-850 | 3 | |
| β-strand | 851-855 | 5 | 2 |
| β-strand | 858-861 | 4 | 2 |
| β-strand | 868-869 | 2 | 3 |
| α-helix | 870-871 | 2 | |
| β-strand | 877-878 | 2 | 4 |
| α-helix | 886-888 | 3 | |
| α-helix | 891-896 | 6 | |
| β-strand | 898-899 | 2 | 4 |
| α-helix | 901-916 | 16 | |
| α-helix | 920-921 | 2 | |
| α-helix | 928-930 | 3 | |
| α-helix | 931-936 | 6 | |
| α-helix | 941-944 | 4 | |
| β-strand | 947 | 1 | 5 |
| α-helix | 949-958 | 10 | |
| α-helix | 963-965 | 3 | |
| α-helix | 967-968 | 2 | |
| α-helix | 969-980 | 12 | |
| α-helix | 983-986 | 4 | |
| β-strand | 987 | 1 | 5 |
| α-helix | 989-992 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 713-714 | 2 | 6 |
| α-helix | 717-719 | 3 | |
| β-strand | 720-729 | 10 | 6 |
| β-strand | 732-739 | 8 | 6 |
| β-strand | 748-755 | 8 | 6 |
| α-helix | 761-775 | 15 | |
| β-strand | 782 | 1 | 7 |
| α-helix | 783-784 | 2 | |
| β-strand | 785-789 | 5 | 6 |
| β-strand | 795-799 | 5 | 6 |
| β-strand | 805 | 1 | 7 |
| α-helix | 806-812 | 7 | |
| α-helix | 819-838 | 20 | |
| β-strand | 841-842 | 2 | 8 |
| α-helix | 848-850 | 3 | |
| β-strand | 851-855 | 5 | 7 |
| β-strand | 858-861 | 4 | 7 |
| β-strand | 868-869 | 2 | 8 |
| α-helix | 870-871 | 2 | |
| β-strand | 877-878 | 2 | 9 |
| α-helix | 886-888 | 3 | |
| α-helix | 891-896 | 6 | |
| β-strand | 898-899 | 2 | 9 |
| α-helix | 901-916 | 16 | |
| α-helix | 920-921 | 2 | |
| α-helix | 928-930 | 3 | |
| α-helix | 931-936 | 6 | |
| α-helix | 941-944 | 4 | |
| β-strand | 947 | 1 | 10 |
| α-helix | 949-958 | 10 | |
| α-helix | 963-965 | 3 | |
| α-helix | 967-968 | 2 | |
| α-helix | 969-981 | 13 | |
| α-helix | 983-986 | 4 | |
| β-strand | 987 | 1 | 10 |
| α-helix | 989-991 | 3 | |
| α-helix | 1003-1007 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Receptor tyrosine-protein kinase erbB-2 | A, B | protein | 338 | Homo sapiens | P04626 (AlphaFold model) |
>3PP0_1 Receptor tyrosine-protein kinase erbB-2 (chains A, B) MSGAAPNQALLRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSP KANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQD LLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADG GKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERL PQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLD STFYRSLLEDDDMGDLVDAEEYLVPQQGAAASHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| 03Q | 2-{2-[4-({5-chloro-6-[3-(trifluoromethyl)phenoxy]pyridin-3-yl}amino)-5H-pyrrolo… | C22 H19 Cl F3 N5 O3 | 2 |
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 P04626 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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