Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K659N Mutation Responsible for an Unclassified Craniosynostosis Syndrome. Determined by X-ray diffraction at 2.2 Å resolution. Released 25 Sept 2007.
Explore 2PVY in 3D Show helices and sheets RCSB PDB PDBe
2PVY contains 74 α-helices and 58 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 | 481-486 | 6 | 1 |
| β-strand | 495-501 | 7 | 1 |
| β-strand | 511-517 | 7 | 1 |
| β-strand | 524 | 1 | 2 |
| α-helix | 525-541 | 17 | |
| 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 | 572-578 | 7 | |
| α-helix | 580-581 | 2 | |
| α-helix | 594-596 | 3 | |
| α-helix | 600-619 | 20 | |
| β-strand | 622-623 | 2 | 4 |
| α-helix | 629-631 | 3 | |
| β-strand | 632-635 | 4 | 3 |
| β-strand | 639-642 | 4 | 3 |
| β-strand | 649-650 | 2 | 4 |
| β-strand | 657-658 | 2 | 5 |
| β-strand | 666 | 1 | 6 |
| α-helix | 667-669 | 3 | |
| α-helix | 672-677 | 6 | |
| β-strand | 679-680 | 2 | 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 |
|---|---|---|---|
| α-helix | 468-470 | 3 | |
| β-strand | 475 | 1 | 7 |
| α-helix | 478-480 | 3 | |
| β-strand | 481-486 | 6 | 7 |
| β-strand | 495-501 | 7 | 7 |
| β-strand | 511-517 | 7 | 7 |
| β-strand | 524 | 1 | 8 |
| α-helix | 525-541 | 17 | |
| β-strand | 547 | 1 | 9 |
| α-helix | 548-549 | 2 | |
| β-strand | 550-554 | 5 | 7 |
| β-strand | 561-565 | 5 | 7 |
| β-strand | 571 | 1 | 9 |
| α-helix | 572-578 | 7 | |
| α-helix | 580-582 | 3 | |
| α-helix | 594-596 | 3 | |
| α-helix | 597-599 | 3 | |
| 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 |
| α-helix | 667-669 | 3 | |
| α-helix | 672-676 | 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 |
|---|---|---|---|
| α-helix | 472-474 | 3 | |
| β-strand | 475 | 1 | 11 |
| α-helix | 478-480 | 3 | |
| β-strand | 481-486 | 6 | 11 |
| β-strand | 495-501 | 7 | 11 |
| β-strand | 511-517 | 7 | 11 |
| β-strand | 524 | 1 | 6 |
| α-helix | 525-539 | 15 | |
| β-strand | 547 | 1 | 12 |
| β-strand | 550-554 | 5 | 11 |
| β-strand | 561-565 | 5 | 11 |
| β-strand | 571 | 1 | 12 |
| α-helix | 572-578 | 7 | |
| α-helix | 580-581 | 2 | |
| α-helix | 597-599 | 3 | |
| α-helix | 600-619 | 20 | |
| β-strand | 622-623 | 2 | 13 |
| α-helix | 629-631 | 3 | |
| β-strand | 632-635 | 4 | 12 |
| β-strand | 639-642 | 4 | 12 |
| β-strand | 649-650 | 2 | 13 |
| β-strand | 666 | 1 | 2 |
| α-helix | 667-669 | 3 | |
| α-helix | 672-676 | 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 | 475 | 1 | 14 |
| α-helix | 478-480 | 3 | |
| β-strand | 481-486 | 6 | 14 |
| β-strand | 495-501 | 7 | 14 |
| β-strand | 511-517 | 7 | 14 |
| α-helix | 525-541 | 17 | |
| β-strand | 547 | 1 | 15 |
| α-helix | 548-549 | 2 | |
| β-strand | 550-554 | 5 | 14 |
| β-strand | 561-565 | 5 | 14 |
| α-helix | 566-567 | 2 | |
| β-strand | 571 | 1 | 15 |
| α-helix | 572-577 | 6 | |
| α-helix | 580-582 | 3 | |
| α-helix | 600-619 | 20 | |
| β-strand | 622-623 | 2 | 16 |
| α-helix | 629-631 | 3 | |
| β-strand | 632-635 | 4 | 15 |
| β-strand | 639-642 | 4 | 15 |
| β-strand | 649-650 | 2 | 16 |
| β-strand | 657-658 | 2 | 17 |
| β-strand | 666 | 1 | 8 |
| α-helix | 667-669 | 3 | |
| α-helix | 672-677 | 6 | |
| β-strand | 679-680 | 2 | 17 |
| 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) |
>2PVY_1 Fibroblast growth factor receptor 2 (chains A, B, C, D) MGSSHHHHHHSQDPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGAFGQVVMAEAVGID KDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIV EYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIH RDLAARNVLVTENNVMKIADFGLARDINNIDYYKNTTNGRLPVKWMAPEALFDRVYTHQS DVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVP SQRPTFKQLVEDLDRILTLTTNEE
| ID | Name | Formula | Copies |
|---|---|---|---|
| ACP | Phosphomethylphosphonic acid adenylate ester | C11 H18 N5 O12 P3 | 4 |
Water and common crystallization additives (SO4) are not listed.
A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases. Chen, H., Ma, J., Li, W. et al. Mol Cell (2007) 27:717-730. DOI 10.1016/j.molcel.2007.06.028 · PubMed
Other PDB entries of the same protein (UniProt P21802 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2PVY 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.