FGFR2 mutant D650V with compound 6. Determined by X-ray diffraction at 1.98 Å resolution. Released 15 Apr 2026.
Explore 10OQ in 3D Show helices and sheets RCSB PDB PDBe
10OQ contains 38 α-helices and 28 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 |
|---|---|---|---|
| α-helix | 457-459 | 3 | |
| α-helix | 461-463 | 3 | |
| β-strand | 470 | 1 | 1 |
| β-strand | 475 | 1 | 2 |
| α-helix | 478-480 | 3 | |
| β-strand | 481-489 | 9 | 2 |
| β-strand | 494-501 | 8 | 2 |
| β-strand | 511-518 | 8 | 2 |
| α-helix | 525-541 | 17 | |
| β-strand | 547 | 1 | 3 |
| β-strand | 550-554 | 5 | 2 |
| β-strand | 561-565 | 5 | 2 |
| β-strand | 571 | 1 | 3 |
| α-helix | 572-578 | 7 | |
| α-helix | 580-581 | 2 | |
| α-helix | 594-596 | 3 | |
| α-helix | 597-599 | 3 | |
| α-helix | 600-619 | 20 | |
| α-helix | 629-631 | 3 | |
| β-strand | 632-634 | 3 | 3 |
| β-strand | 640-642 | 3 | 3 |
| β-strand | 651 | 1 | 4 |
| α-helix | 666-669 | 4 | |
| α-helix | 672-677 | 6 | |
| β-strand | 679 | 1 | 5 |
| α-helix | 682-697 | 16 | |
| α-helix | 701-702 | 2 | |
| α-helix | 709-717 | 9 | |
| α-helix | 722-725 | 4 | |
| α-helix | 730-739 | 10 | |
| α-helix | 744-746 | 3 | |
| α-helix | 748-749 | 2 | |
| α-helix | 750-763 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 459 | 1 | 6 |
| α-helix | 460-462 | 3 | |
| α-helix | 464-466 | 3 | |
| β-strand | 467 | 1 | 4 |
| α-helix | 468-469 | 2 | |
| β-strand | 470 | 1 | 5 |
| β-strand | 475 | 1 | 7 |
| α-helix | 478-480 | 3 | |
| β-strand | 481-489 | 9 | 7 |
| β-strand | 494-501 | 8 | 7 |
| β-strand | 511-517 | 7 | 7 |
| β-strand | 524 | 1 | 6 |
| α-helix | 525-541 | 17 | |
| β-strand | 547 | 1 | 8 |
| β-strand | 550-554 | 5 | 7 |
| β-strand | 561-565 | 5 | 7 |
| β-strand | 571 | 1 | 8 |
| α-helix | 572-578 | 7 | |
| α-helix | 600-619 | 20 | |
| α-helix | 629-631 | 3 | |
| β-strand | 632-634 | 3 | 8 |
| β-strand | 640-642 | 3 | 8 |
| α-helix | 666-669 | 4 | |
| α-helix | 672-677 | 6 | |
| β-strand | 679 | 1 | 1 |
| α-helix | 682-697 | 16 | |
| α-helix | 701-702 | 2 | |
| α-helix | 709-717 | 9 | |
| α-helix | 722-725 | 4 | |
| α-helix | 730-739 | 10 | |
| α-helix | 744-746 | 3 | |
| α-helix | 748-749 | 2 | |
| α-helix | 750-763 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fibroblast growth factor receptor 2 | A, B | protein | 324 | Homo sapiens | P21802 (AlphaFold model) |
>10OQ_1 Fibroblast growth factor receptor 2 (chains A, B) MGSSHHHHHHSQDPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGID KDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIV EYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIH RDLAARNVLVTENNVMKIADFGLARVINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQS DVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVP SQRPTFKQLVEDLDRILTLTTNEE
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1C66 | N-[(3M)-3-{5-chloro-2-[4-(morpholin-4-yl)anilino]pyrimidin-4-yl}-1-methyl-1H-in… | C26 H27 Cl N6 O2 | 2 |
Water and common crystallization additives (SO4, GOL) are not listed.
Structure-Based Design of a Novel Covalent 4-(1-Methylindol-3-yl)pyrimidin-2-amine Series Targeting FGFR2 Resistance Mutations. Hudkins, R.L., Allen, E., Iyer, S. et al. J Med Chem (2026) 69:8614-8627. DOI 10.1021/acs.jmedchem.6c00514 · PubMed
Other PDB entries of the same protein (UniProt P21802 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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