FGFR1 kinase domain (residues 458-765) with mutations C488A, C584S in complex with 38. Determined by X-ray diffraction at 1.71 Å resolution. Released 1 Dec 2021.
Explore 7OZB in 3D Show helices and sheets RCSB PDB PDBe
7OZB contains 37 α-helices and 22 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 | 465-467 | 3 | |
| β-strand | 472 | 1 | 1 |
| α-helix | 475-477 | 3 | |
| β-strand | 478-483 | 6 | 1 |
| β-strand | 492-498 | 7 | 1 |
| β-strand | 508-514 | 7 | 1 |
| α-helix | 522-538 | 17 | |
| β-strand | 544 | 1 | 2 |
| β-strand | 547-551 | 5 | 1 |
| β-strand | 558-562 | 5 | 1 |
| β-strand | 568 | 1 | 2 |
| α-helix | 569-575 | 7 | |
| α-helix | 597-616 | 20 | |
| α-helix | 626-628 | 3 | |
| β-strand | 629-631 | 3 | 2 |
| β-strand | 637-639 | 3 | 2 |
| α-helix | 648-650 | 3 | |
| α-helix | 655-657 | 3 | |
| α-helix | 663-666 | 4 | |
| α-helix | 669-674 | 6 | |
| α-helix | 679-694 | 16 | |
| α-helix | 706-714 | 9 | |
| α-helix | 719-721 | 3 | |
| β-strand | 722 | 1 | 3 |
| 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 | 4 |
| α-helix | 475-477 | 3 | |
| β-strand | 478-486 | 9 | 4 |
| β-strand | 490-498 | 9 | 4 |
| β-strand | 508-516 | 9 | 4 |
| α-helix | 522-538 | 17 | |
| β-strand | 544 | 1 | 5 |
| α-helix | 545-546 | 2 | |
| β-strand | 547-551 | 5 | 4 |
| β-strand | 558-562 | 5 | 4 |
| β-strand | 568 | 1 | 5 |
| α-helix | 569-574 | 6 | |
| α-helix | 594-596 | 3 | |
| α-helix | 597-616 | 20 | |
| α-helix | 626-628 | 3 | |
| β-strand | 629-631 | 3 | 5 |
| β-strand | 637-639 | 3 | 5 |
| α-helix | 648-650 | 3 | |
| α-helix | 655-657 | 3 | |
| α-helix | 663-666 | 4 | |
| α-helix | 669-673 | 5 | |
| α-helix | 679-694 | 16 | |
| α-helix | 698-699 | 2 | |
| α-helix | 706-714 | 9 | |
| α-helix | 719-721 | 3 | |
| β-strand | 722 | 1 | 3 |
| α-helix | 727-736 | 10 | |
| α-helix | 741-743 | 3 | |
| α-helix | 745-746 | 2 | |
| α-helix | 747-759 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fibroblast growth factor receptor 1 | AAA, BBB | protein | 309 | Homo sapiens | P11362 (AlphaFold model) |
>7OZB_1 Fibroblast growth factor receptor 1 (chains AAA, BBB) GAGVSEYELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLDKDKPNRVTKVAVKML KSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQAR RPPGLEYSYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNV MKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTL GGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDR IVALTSNQE
| ID | Name | Formula | Copies |
|---|---|---|---|
| 47I | 4-[3-(4-piperazin-4-ium-1-ylphenyl)-1H-indazol-6-yl]phenol | C23 H23 N4 O | 2 |
Water and common crystallization additives (EDO, SO4) are not listed.
From Fragment to Lead: De Novo Design and Development toward a Selective FGFR2 Inhibitor. Turner, L.D., Trinh, C.H., Hubball, R.A. et al. J Med Chem (2022) 65:1481-1504. DOI 10.1021/acs.jmedchem.1c01163 · PubMed
Other PDB entries of the same protein (UniProt P11362 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 7OZB directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.