Crystal Structure of D. melanogaster Ssu72+Symplekin bound to cis peptidomimetic CTD phospho-Ser5 peptide. Determined by X-ray diffraction at 2.95 Å resolution. Released 16 Sept 2015.
Explore 4YGX in 3D Show helices and sheets RCSB PDB PDBe
4YGX contains 63 α-helices and 16 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 |
|---|---|---|---|
| α-helix | 22-37 | 16 | |
| α-helix | 42-54 | 13 | |
| α-helix | 55-59 | 5 | |
| α-helix | 61-64 | 4 | |
| α-helix | 68-72 | 5 | |
| α-helix | 73-75 | 3 | |
| α-helix | 80-96 | 17 | |
| α-helix | 98-100 | 3 | |
| α-helix | 101-111 | 11 | |
| α-helix | 117-138 | 22 | |
| α-helix | 146-164 | 19 | |
| α-helix | 165-167 | 3 | |
| α-helix | 171-187 | 17 | |
| α-helix | 204-206 | 3 | |
| α-helix | 216-234 | 19 | |
| α-helix | 241-257 | 17 | |
| α-helix | 259-261 | 3 | |
| α-helix | 262-274 | 13 | |
| α-helix | 282-300 | 19 | |
| α-helix | 303-308 | 6 | |
| α-helix | 309-318 | 10 | |
| α-helix | 323-329 | 7 | |
| α-helix | 331-332 | 2 | |
| α-helix | 335-349 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-13 | 6 | 1 |
| α-helix | 19-28 | 10 | |
| β-strand | 33-38 | 6 | 1 |
| β-strand | 43-45 | 3 | 2 |
| β-strand | 54-56 | 3 | 2 |
| α-helix | 62-73 | 12 | |
| α-helix | 76-79 | 4 | |
| α-helix | 82-92 | 11 | |
| β-strand | 98 | 1 | 1 |
| β-strand | 108-111 | 4 | 1 |
| α-helix | 114-126 | 13 | |
| α-helix | 128-129 | 2 | |
| β-strand | 134-139 | 6 | 1 |
| α-helix | 146-164 | 19 | |
| α-helix | 169-183 | 15 | |
| β-strand | 189-194 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 43-53 | 11 | |
| α-helix | 54-59 | 6 | |
| α-helix | 61-64 | 4 | |
| α-helix | 68-72 | 5 | |
| α-helix | 73-76 | 4 | |
| α-helix | 80-96 | 17 | |
| α-helix | 98-100 | 3 | |
| α-helix | 101-111 | 11 | |
| α-helix | 117-138 | 22 | |
| α-helix | 146-164 | 19 | |
| α-helix | 165-167 | 3 | |
| α-helix | 171-187 | 17 | |
| α-helix | 204-206 | 3 | |
| α-helix | 216-234 | 19 | |
| α-helix | 241-257 | 17 | |
| α-helix | 259-261 | 3 | |
| α-helix | 262-274 | 13 | |
| α-helix | 282-300 | 19 | |
| α-helix | 303-308 | 6 | |
| α-helix | 309-318 | 10 | |
| α-helix | 323-329 | 7 | |
| α-helix | 331-332 | 2 | |
| α-helix | 335-349 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-13 | 6 | 3 |
| α-helix | 19-29 | 11 | |
| β-strand | 33-38 | 6 | 3 |
| β-strand | 43-45 | 3 | 4 |
| β-strand | 54-56 | 3 | 4 |
| α-helix | 62-73 | 12 | |
| α-helix | 76-79 | 4 | |
| α-helix | 82-92 | 11 | |
| β-strand | 98 | 1 | 3 |
| α-helix | 99-101 | 3 | |
| β-strand | 108-111 | 4 | 3 |
| α-helix | 114-126 | 13 | |
| β-strand | 134-139 | 6 | 3 |
| α-helix | 146-164 | 19 | |
| α-helix | 169-183 | 15 | |
| β-strand | 189-194 | 6 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Symplekin | A, C | protein | 339 | Drosophila melanogaster | Q8MSU4 (AlphaFold model) |
| LD40846p | B, D | protein | 200 | Drosophila melanogaster | Q9VWE4 (AlphaFold model) |
| cis peptidomimetic CTD phospho-Ser5 peptide | E | protein | 12 | synthetic construct |
>4YGX_1 Symplekin (chains A, C) GPGSGMTDEKTATARAKVVDWCNELVIASPSTKCELLAKVQETVLGSCAELAEEFLESVL SLAHDSNMEVRKQVVAFVEQVCKVKVELLPHVINVVSMLLRDNSAQVIKRVIQACGSIYK NGLQYLCSLMEPGDSAEQAWNILSLIKAQILDMIDNENDGIRTNAIKFLEGVVVLQSFAD EDSLKRDGDFSLADVPDHCTLFRREKLQEEGNNILDILLQFHGTTHISSVNLIACTSSLC TIAKMRPIFMGAVVEAFKQLNANLPPTLTDSQVSSVRKSLKMQLQTLLKNRGAFEFASTI RGMLVDLGSSTNEIQKLIPKMDKQEMARRQKRILENAAQ
>4YGX_2 LD40846p (chains B, D) GPGSGMTDPSKLAVAVVDSSNMNRSMEAHNFLAKKGFNVRSYGTGERVKLPGMAFDKPNV YEFGTKYEDIYRDLESKDKEFYTQNGLLHMLDRNRRIKKCPERFQDTKEQFDIIVTVEER VYDLVVMHMESMESVDNRPVHVLNVDVVNNAEDALMGAFVITDMINMMAKSTDLDNDIDE LIQEFEERRKRVILHSVLFY
>4YGX_3 cis peptidomimetic CTD phospho-Ser5 peptide (chains E) XSPYSPTXSYSX
Chemical Tools To Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II. Mayfield, J.E., Fan, S., Wei, S. et al. ACS Chem Biol (2015) 10:2405-2414. DOI 10.1021/acschembio.5b00296 · PubMed
Other PDB entries of the same protein (UniProt Q8MSU4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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