Structure of phosphotransferase. Determined by X-ray diffraction at 1.8 Å resolution. Released 26 Feb 2008.
Explore 3B2T in 3D Show helices and sheets RCSB PDB PDBe
3B2T contains 37 α-helices and 28 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 | 468-470 | 3 | |
| α-helix | 472-474 | 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 | 525-541 | 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 | 572-577 | 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 |
| β-strand | 649-650 | 2 | 4 |
| β-strand | 666 | 1 | 5 |
| 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 | 750-764 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 459-460 | 2 | |
| α-helix | 468-470 | 3 | |
| α-helix | 472-474 | 3 | |
| β-strand | 475 | 1 | 6 |
| α-helix | 478-480 | 3 | |
| β-strand | 481-486 | 6 | 6 |
| β-strand | 494-501 | 8 | 6 |
| β-strand | 511-518 | 8 | 6 |
| β-strand | 524 | 1 | 5 |
| α-helix | 525-541 | 17 | |
| 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 |
| β-strand | 649-650 | 2 | 8 |
| 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 | 750-762 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fibroblast growth factor receptor 2 | A, B | protein | 311 | Homo sapiens | P21802 (AlphaFold model) |
>3B2T_1 Fibroblast growth factor receptor 2 (chains A, B) PMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVK MLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLR ARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLTARNVLVTEN NVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIF TLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDL DRILTLTTNQE
| ID | Name | Formula | Copies |
|---|---|---|---|
| M33 | 5'-O-[(S)-hydroxy{[(S)-hydroxy(methyl)phosphoryl]oxy}phosphoryl]adenosine | C11 H17 N5 O9 P2 | 2 |
| PO4 | Phosphate ion | O4 P | 4 |
Structural basis for reduced FGFR2 activity in LADD syndrome: Implications for FGFR autoinhibition and activation. Lew, E.D., Bae, J.H., Rohmann, E. et al. Proc Natl Acad Sci U S A (2007) 104:19802-19807. DOI 10.1073/pnas.0709905104 · 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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