Tgf-beta receptor type 2 kinase domain (E431A,R433A,E485A,K488A,R493A,R495A). Determined by X-ray diffraction at 1.69 Å resolution. Released 11 May 2016.
Explore 5E8V in 3D Show helices and sheets RCSB PDB PDBe
5E8V contains 21 α-helices and 15 β-strands across 1 chain. 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 | 244-252 | 9 | 1 |
| β-strand | 257-263 | 7 | 1 |
| β-strand | 273-280 | 8 | 1 |
| α-helix | 281-283 | 3 | |
| α-helix | 284-294 | 11 | |
| α-helix | 297-299 | 3 | |
| β-strand | 304 | 1 | 2 |
| α-helix | 305-306 | 2 | |
| β-strand | 307-314 | 8 | 1 |
| β-strand | 319-326 | 8 | 1 |
| β-strand | 332 | 1 | 2 |
| α-helix | 333-339 | 7 | |
| α-helix | 341 | 1 | |
| β-strand | 342 | 1 | 3 |
| α-helix | 343 | 1 | |
| α-helix | 344-362 | 19 | |
| β-strand | 365 | 1 | 4 |
| β-strand | 371 | 1 | 4 |
| β-strand | 375-376 | 2 | 5 |
| α-helix | 382-384 | 3 | |
| β-strand | 385-387 | 3 | 2 |
| β-strand | 393-395 | 3 | 2 |
| β-strand | 402-403 | 2 | 5 |
| α-helix | 422-424 | 3 | |
| α-helix | 427-430 | 4 | |
| α-helix | 439-459 | 21 | |
| β-strand | 461 | 1 | 3 |
| α-helix | 462-464 | 3 | |
| α-helix | 467-470 | 4 | |
| α-helix | 484-488 | 5 | |
| α-helix | 489-493 | 5 | |
| α-helix | 502-506 | 5 | |
| α-helix | 508-520 | 13 | |
| α-helix | 525-527 | 3 | |
| α-helix | 529-530 | 2 | |
| α-helix | 531-540 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| TGF-beta receptor type-2 | A | protein | 316 | Homo sapiens | P37173 (AlphaFold model) |
>5E8V_1 TGF-beta receptor type-2 (chains A) GHMHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYASWKTEKDI FSDINLKHENILQFLTAEERKTELGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSS LARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDL ANSGQVGTARYMAPEVLASAMNLENVESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPP FGSKVREHPCVASMADNVLADAGRPEIPSFWLNHQGIQMVCETLTECWDHDPEARLTAQC VAERFSELEHLDRLSG
Crystal structures of apo and inhibitor-bound TGF beta R2 kinase domain: insights into TGF beta R isoform selectivity. Tebben, A.J., Ruzanov, M., Gao, M. et al. Acta Crystallogr D Struct Biol (2016) 72:658-674. DOI 10.1107/S2059798316003624 · PubMed
Other PDB entries of the same protein (UniProt P37173 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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