Crystal Structure of Human Rtf1 Plus3 domain. Determined by X-ray diffraction at 2.12 Å resolution. Released 2 Oct 2013.
Explore 4L1P in 3D Show helices and sheets RCSB PDB PDBe
4L1P contains 19 α-helices and 18 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 | 352 | 1 | 4 |
| α-helix | 356-359 | 4 | |
| α-helix | 360-362 | 3 | |
| β-strand | 363 | 1 | 2 |
| α-helix | 364-365 | 2 | |
| α-helix | 366-372 | 7 | |
| α-helix | 378-382 | 5 | |
| β-strand | 386-390 | 5 | 2 |
| β-strand | 400-417 | 18 | 2 |
| β-strand | 420-430 | 11 | 2 |
| β-strand | 433-438 | 6 | 2 |
| α-helix | 439-441 | 3 | |
| β-strand | 442 | 1 | 2 |
| α-helix | 446-448 | 3 | |
| α-helix | 449-462 | 14 | |
| α-helix | 465-467 | 3 | |
| β-strand | 468 | 1 | 4 |
| α-helix | 469-481 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 352 | 1 | 1 |
| α-helix | 356-359 | 4 | |
| α-helix | 360-362 | 3 | |
| β-strand | 363 | 1 | 2 |
| α-helix | 366-372 | 7 | |
| α-helix | 378-382 | 5 | |
| β-strand | 383 | 1 | 3 |
| β-strand | 385 | 1 | 3 |
| β-strand | 386-393 | 8 | 2 |
| β-strand | 398-417 | 20 | 2 |
| β-strand | 420-430 | 11 | 2 |
| β-strand | 433-438 | 6 | 2 |
| α-helix | 439-441 | 3 | |
| β-strand | 442 | 1 | 2 |
| α-helix | 446-448 | 3 | |
| α-helix | 449-462 | 14 | |
| α-helix | 465-467 | 3 | |
| β-strand | 468 | 1 | 1 |
| α-helix | 469-481 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RNA polymerase-associated protein RTF1 homolog | A, B | protein | 138 | Homo sapiens | Q92541 (AlphaFold model) |
>4L1P_1 RNA polymerase-associated protein RTF1 homolog (chains A, B) GDITHMVSLPEELNRVRLSRHKLERWCHMPFFAKTVTGCFVRIGIGNHNSKPVYRVAEIT GVVETAKVYQLGGTRTNKGLQLRHGNDQRVFRLEFVSNQEFTESEFMKWKEAMFSAGMQL PTLDEINKKELSIKEALN
Structural basis for Spt5-mediated recruitment of the Paf1 complex to chromatin. Wier, A.D., Mayekar, M.K., Heroux, A. et al. Proc Natl Acad Sci U S A (2013) 110:17290-17295. DOI 10.1073/pnas.1314754110 · PubMed
Other PDB entries of the same protein (UniProt Q92541 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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