Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation. Determined by X-ray diffraction at 1.85 Å resolution. Released 7 Aug 2013.
Explore 4J99 in 3D Show helices and sheets RCSB PDB PDBe
4J99 contains 68 α-helices and 66 β-strands across 4 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 | 1 |
| α-helix | 478-480 | 3 | |
| β-strand | 481-489 | 9 | 1 |
| β-strand | 494-501 | 8 | 1 |
| β-strand | 510 | 1 | 2 |
| β-strand | 511-518 | 8 | 1 |
| β-strand | 524 | 1 | 3 |
| α-helix | 525-540 | 16 | |
| β-strand | 547 | 1 | 4 |
| α-helix | 548-549 | 2 | |
| β-strand | 550-554 | 5 | 1 |
| β-strand | 561-565 | 5 | 1 |
| β-strand | 571 | 1 | 4 |
| α-helix | 572-577 | 6 | |
| α-helix | 600-619 | 20 | |
| β-strand | 622-623 | 2 | 5 |
| α-helix | 629-631 | 3 | |
| β-strand | 632-634 | 3 | 4 |
| β-strand | 640-642 | 3 | 4 |
| β-strand | 649-650 | 2 | 5 |
| β-strand | 657-658 | 2 | 6 |
| β-strand | 666 | 1 | 7 |
| α-helix | 667-669 | 3 | |
| α-helix | 672-677 | 6 | |
| β-strand | 679-680 | 2 | 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 475 | 1 | 8 |
| α-helix | 478-480 | 3 | |
| β-strand | 481-489 | 9 | 8 |
| β-strand | 494-501 | 8 | 8 |
| β-strand | 511-518 | 8 | 8 |
| β-strand | 524 | 1 | 7 |
| α-helix | 525-541 | 17 | |
| β-strand | 547 | 1 | 9 |
| α-helix | 548-549 | 2 | |
| β-strand | 550-554 | 5 | 8 |
| β-strand | 561-565 | 5 | 8 |
| β-strand | 571 | 1 | 9 |
| α-helix | 572-577 | 6 | |
| α-helix | 580-581 | 2 | |
| α-helix | 600-619 | 20 | |
| β-strand | 622-623 | 2 | 10 |
| α-helix | 629-631 | 3 | |
| β-strand | 632-634 | 3 | 9 |
| β-strand | 640-642 | 3 | 9 |
| β-strand | 649-650 | 2 | 10 |
| β-strand | 657-658 | 2 | 11 |
| α-helix | 659-660 | 2 | |
| β-strand | 666 | 1 | 3 |
| α-helix | 667-669 | 3 | |
| α-helix | 672-677 | 6 | |
| β-strand | 679-680 | 2 | 11 |
| 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 | 475 | 1 | 12 |
| α-helix | 478-480 | 3 | |
| β-strand | 481-489 | 9 | 12 |
| β-strand | 494-501 | 8 | 12 |
| β-strand | 511-518 | 8 | 12 |
| β-strand | 524 | 1 | 13 |
| α-helix | 525-541 | 17 | |
| β-strand | 547 | 1 | 14 |
| α-helix | 548-549 | 2 | |
| β-strand | 550-554 | 5 | 12 |
| β-strand | 561-565 | 5 | 12 |
| β-strand | 571 | 1 | 14 |
| α-helix | 572-577 | 6 | |
| α-helix | 580-581 | 2 | |
| α-helix | 600-619 | 20 | |
| β-strand | 622-623 | 2 | 15 |
| α-helix | 629-631 | 3 | |
| β-strand | 632-634 | 3 | 14 |
| β-strand | 640-642 | 3 | 14 |
| β-strand | 649-650 | 2 | 15 |
| β-strand | 657-658 | 2 | 16 |
| α-helix | 659-660 | 2 | |
| β-strand | 666 | 1 | 17 |
| α-helix | 667-669 | 3 | |
| α-helix | 672-677 | 6 | |
| β-strand | 679-680 | 2 | 16 |
| 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 |
|---|---|---|---|
| β-strand | 475 | 1 | 18 |
| α-helix | 478-480 | 3 | |
| β-strand | 481-489 | 9 | 18 |
| β-strand | 494-501 | 8 | 18 |
| β-strand | 510 | 1 | 2 |
| β-strand | 511-518 | 8 | 18 |
| β-strand | 524 | 1 | 17 |
| α-helix | 525-541 | 17 | |
| β-strand | 547 | 1 | 19 |
| α-helix | 548-549 | 2 | |
| β-strand | 550-554 | 5 | 18 |
| β-strand | 561-565 | 5 | 18 |
| β-strand | 571 | 1 | 19 |
| α-helix | 572-577 | 6 | |
| α-helix | 600-619 | 20 | |
| β-strand | 622-623 | 2 | 20 |
| α-helix | 629-631 | 3 | |
| β-strand | 632-634 | 3 | 19 |
| β-strand | 640-642 | 3 | 19 |
| β-strand | 649-650 | 2 | 20 |
| β-strand | 657-658 | 2 | 21 |
| β-strand | 666 | 1 | 13 |
| α-helix | 667-669 | 3 | |
| α-helix | 672-677 | 6 | |
| β-strand | 679-680 | 2 | 21 |
| 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, C, D | protein | 324 | Homo sapiens | P21802 (AlphaFold model) |
>4J99_1 Fibroblast growth factor receptor 2 (chains A, B, C, D) MGSSHHHHHHSQDPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGAFGQVVMAEAVGID KDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIV EYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIH RDLAARNVLVTENNVMKIADFGLARDINNIDYYKTTTNGRLPVKWMAPEALFDRVYTHQS DVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVP SQRPTFKQLVEDLDRILTLTTNEE
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 3 |
| ACP | Phosphomethylphosphonic acid adenylate ester | C11 H18 N5 O12 P3 | 4 |
Water and common crystallization additives (SO4) are not listed.
Cracking the Molecular Origin of Intrinsic Tyrosine Kinase Activity through Analysis of Pathogenic Gain-of-Function Mutations. Chen, H., Huang, Z., Dutta, K. et al. Cell Rep (2013) 4:376-384. DOI 10.1016/j.celrep.2013.06.025 · 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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