Crystal Structure of FGF Receptor 2 Tyrosine Kinase Domain Harboring the D650V Activating Mutation. Determined by X-ray diffraction at 1.86 Å resolution. Released 22 Feb 2017.
Explore 5UGL in 3D Show helices and sheets RCSB PDB PDBe
5UGL contains 36 α-helices and 30 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 | 475 | 1 | 6 |
| α-helix | 478-480 | 3 | |
| β-strand | 481-489 | 9 | 6 |
| β-strand | 494-501 | 8 | 6 |
| β-strand | 511-518 | 8 | 6 |
| β-strand | 524 | 1 | 5 |
| α-helix | 525-540 | 16 | |
| β-strand | 547 | 1 | 7 |
| α-helix | 548-549 | 2 | |
| β-strand | 550-554 | 5 | 6 |
| β-strand | 561-565 | 5 | 6 |
| β-strand | 571 | 1 | 7 |
| α-helix | 572-577 | 6 | |
| α-helix | 600-619 | 20 | |
| β-strand | 622-623 | 2 | 8 |
| α-helix | 629-631 | 3 | |
| β-strand | 632-634 | 3 | 7 |
| β-strand | 640-642 | 3 | 7 |
| α-helix | 645-647 | 3 | |
| β-strand | 649-650 | 2 | 8 |
| α-helix | 655 | 1 | |
| β-strand | 656-657 | 2 | 9 |
| β-strand | 666 | 1 | 2 |
| α-helix | 667-669 | 3 | |
| α-helix | 672-677 | 6 | |
| β-strand | 679-680 | 2 | 9 |
| 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 | 750-762 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 468-470 | 3 | |
| β-strand | 475 | 1 | 1 |
| α-helix | 478-480 | 3 | |
| β-strand | 481-489 | 9 | 1 |
| β-strand | 494-501 | 8 | 1 |
| β-strand | 511-518 | 8 | 1 |
| β-strand | 524 | 1 | 2 |
| α-helix | 525-540 | 16 | |
| β-strand | 547 | 1 | 3 |
| α-helix | 548-549 | 2 | |
| β-strand | 550-554 | 5 | 1 |
| β-strand | 561-565 | 5 | 1 |
| β-strand | 571 | 1 | 3 |
| α-helix | 572-577 | 6 | |
| α-helix | 600-619 | 20 | |
| β-strand | 622-623 | 2 | 4 |
| α-helix | 629-631 | 3 | |
| β-strand | 632-634 | 3 | 3 |
| β-strand | 640-642 | 3 | 3 |
| α-helix | 645-647 | 3 | |
| β-strand | 649-650 | 2 | 4 |
| β-strand | 666 | 1 | 5 |
| α-helix | 667-669 | 3 | |
| α-helix | 672-677 | 6 | |
| 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 | 750-762 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fibroblast growth factor receptor 2 | A, B | protein | 324 | Homo sapiens | P21802 (AlphaFold model) |
>5UGL_1 Fibroblast growth factor receptor 2 (chains A, B) MGSSHHHHHHSQDPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGAFGQVVMAEAVGID KDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIV EYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIH RDLAARNVLVTENNVMKIADFGLARVINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQS DVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVP SQRPTFKQLVEDLDRILTLTTNEE
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
Water and common crystallization additives (SO4) are not listed.
Elucidation of a four-site allosteric network in fibroblast growth factor receptor tyrosine kinases. Chen, H., Marsiglia, W.M., Cho, M.K. et al. Elife (2017) 6. DOI 10.7554/eLife.21137 · 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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