FGFR1 kinase domain with a covalent inhibitor 10h. Determined by X-ray diffraction at 1.75 Å resolution. Released 26 Jun 2024.
Explore 8XZ7 in 3D Show helices and sheets RCSB PDB PDBe
8XZ7 contains 39 α-helices and 24 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 | 459-462 | 4 | |
| α-helix | 465-467 | 3 | |
| β-strand | 472 | 1 | 3 |
| α-helix | 475-477 | 3 | |
| β-strand | 478-483 | 6 | 3 |
| α-helix | 484 | 1 | |
| β-strand | 491-498 | 8 | 3 |
| β-strand | 501 | 1 | 4 |
| β-strand | 504 | 1 | 4 |
| β-strand | 508-515 | 8 | 3 |
| α-helix | 522-538 | 17 | |
| β-strand | 544 | 1 | 5 |
| α-helix | 545-546 | 2 | |
| β-strand | 547-551 | 5 | 3 |
| β-strand | 558-562 | 5 | 3 |
| β-strand | 568 | 1 | 5 |
| α-helix | 569-575 | 7 | |
| α-helix | 597-616 | 20 | |
| β-strand | 619 | 1 | 6 |
| α-helix | 626-628 | 3 | |
| β-strand | 629-631 | 3 | 5 |
| β-strand | 637-639 | 3 | 5 |
| β-strand | 644 | 1 | 6 |
| α-helix | 655-657 | 3 | |
| α-helix | 663-666 | 4 | |
| α-helix | 669-674 | 6 | |
| α-helix | 679-694 | 16 | |
| α-helix | 706-715 | 10 | |
| α-helix | 719-722 | 4 | |
| α-helix | 727-736 | 10 | |
| α-helix | 741-743 | 3 | |
| α-helix | 745-746 | 2 | |
| α-helix | 747-760 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 465-467 | 3 | |
| β-strand | 472 | 1 | 1 |
| α-helix | 475-477 | 3 | |
| β-strand | 478-483 | 6 | 1 |
| α-helix | 484 | 1 | |
| β-strand | 491-498 | 8 | 1 |
| β-strand | 508-515 | 8 | 1 |
| α-helix | 522-538 | 17 | |
| β-strand | 544 | 1 | 2 |
| α-helix | 545-546 | 2 | |
| β-strand | 547-551 | 5 | 1 |
| β-strand | 558-562 | 5 | 1 |
| β-strand | 568 | 1 | 2 |
| α-helix | 569-574 | 6 | |
| α-helix | 593-596 | 4 | |
| α-helix | 597-616 | 20 | |
| α-helix | 626-628 | 3 | |
| β-strand | 629-631 | 3 | 2 |
| β-strand | 637-639 | 3 | 2 |
| α-helix | 644-647 | 4 | |
| α-helix | 663-666 | 4 | |
| α-helix | 669-674 | 6 | |
| α-helix | 679-694 | 16 | |
| α-helix | 698-699 | 2 | |
| α-helix | 706-715 | 10 | |
| α-helix | 719-722 | 4 | |
| α-helix | 727-736 | 10 | |
| α-helix | 741-743 | 3 | |
| α-helix | 745-746 | 2 | |
| α-helix | 747-760 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fibroblast growth factor receptor 1 | A, B | protein | 310 | Homo sapiens | P11362 (AlphaFold model) |
>8XZ7_1 Fibroblast growth factor receptor 1 (chains A, B) GPAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKM LKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQA RRPPGLEYSYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDN VMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFT LGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLD RIVALTSNQE
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1LWW | 5-azanyl-3-[2-[4,6-bis(fluoranyl)-2-methyl-3~{H}-benzimidazol-5-yl]ethynyl]-1-[… | C24 H19 F2 N7 O2 | 2 |
Water and common crystallization additives (SO4) are not listed.
Design, synthesis and biological evaluation of 5-amino-1H-pyrazole-4-carboxamide derivatives as pan-FGFR covalent inhibitors. Deng, W., Chen, X., Liang, H. et al. Eur J Med Chem (2024) 275:116558-116558. DOI 10.1016/j.ejmech.2024.116558 · PubMed
Other PDB entries of the same protein (UniProt P11362 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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