Novel Modifications on C-terminal Domain of RNA Polymerase II can Fine-tune the Phosphatase Activity of Ssu72. Determined by X-ray diffraction at 2.58 Å resolution. Released 7 Aug 2013.
Explore 4IMJ in 3D Show helices and sheets RCSB PDB PDBe
4IMJ contains 64 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 |
| α-helix | 99-101 | 3 | |
| 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 | 43-54 | 12 | |
| 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 | 3 |
| α-helix | 19-28 | 10 | |
| β-strand | 33-38 | 6 | 3 |
| β-strand | 43-49 | 7 | 4 |
| β-strand | 52-56 | 5 | 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) |
| CG14216 | B, D | protein | 200 | Drosophila melanogaster | Q9VWE4 (AlphaFold model) |
| CTD | F | protein | 19 | Synthetic |
>4IMJ_1 Symplekin (chains A, C) GPGSGMTDEKTATARAKVVDWCNELVIASPSTKCELLAKVQETVLGSCAELAEEFLESVL SLAHDSNMEVRKQVVAFVEQVCKVKVELLPHVINVVSMLLRDNSAQVIKRVIQACGSIYK NGLQYLCSLMEPGDSAEQAWNILSLIKAQILDMIDNENDGIRTNAIKFLEGVVVLQSFAD EDSLKRDGDFSLADVPDHCTLFRREKLQEEGNNILDILLQFHGTTHISSVNLIACTSSLC TIAKMRPIFMGAVVEAFKQLNANLPPTLTDSQVSSVRKSLKMQLQTLLKNRGAFEFASTI RGMLVDLGSSTNEIQKLIPKMDKQEMARRQKRILENAAQ
>4IMJ_2 CG14216 (chains B, D) GPGSGMTDPSKLAVAVVDSSNMNRSMEAHNFLAKKGFNVRSYGTGERVKLPGMAFDKPNV YEFGTKYEDIYRDLESKDKEFYTQNGLLHMLDRNRRIKKCPERFQDTKEQFDIIVTVEER VYDLVVMHMESMESVDNRPVHVLNVDVVNNAEDALMGAFVITDMINMMAKSTDLDNDIDE LIQEFEERRKRVILHSVLFY
>4IMJ_3 CTD (chains F) SPSYSPTSPSYSPTSPSYS
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 1 |
Novel Modifications on C-terminal Domain of RNA Polymerase II Can Fine-tune the Phosphatase Activity of Ssu72. Luo, Y., Yogesha, S.D., Cannon, J.R. et al. ACS Chem Biol (2013) 8:2042-2052. DOI 10.1021/cb400229c · 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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