4IMI: Symplekin
Novel Modifications on C-terminal Domain of RNA Polymerase II can Fine- tune the Phosphatase Activity of Ssu72. Determined by X-ray diffraction at 2.35 Å resolution. Released 7 Aug 2013.
- Method
- X-ray diffraction
- Resolution
- 2.35 Å
- Organisms
- Drosophila melanogaster, Synthetic
- Chains
- 5
- Atoms
- 8,381
- Mol. weight
- 123.49 kDa
- Ligands
- PO4
- Released
- 7 Aug 2013
Explore 4IMI in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4IMI contains 64 α-helices and 16 β-strands across 5 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.
Chain A: 24 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 22-37 | 16 | |
| α-helix | 42-54 | 13 | |
| α-helix | 55-59 | 5 | |
| α-helix | 61-67 | 7 | |
| α-helix | 68-72 | 5 | |
| α-helix | 73-75 | 3 | |
| α-helix | 80-96 | 17 | |
| α-helix | 98-103 | 6 | |
| α-helix | 105-111 | 7 | |
| α-helix | 117-140 | 24 | |
| 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 | 323-327 | 5 | |
| α-helix | 331-332 | 2 | |
| α-helix | 335-348 | 14 | |
Chain B: 8 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-13 | 6 | 1 |
| α-helix | 19-29 | 11 | |
| 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 | |
| β-strand | 134-139 | 6 | 1 |
| α-helix | 146-165 | 20 | |
| α-helix | 169-184 | 16 | |
| β-strand | 190-194 | 5 | 1 |
Chain C: 23 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 43-53 | 11 | |
| α-helix | 54-59 | 6 | |
| α-helix | 61-65 | 5 | |
| 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 | 117-140 | 24 | |
| 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 | 323-327 | 5 | |
| α-helix | 331-332 | 2 | |
| α-helix | 335-348 | 14 | |
Chain D: 8 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-13 | 6 | 3 |
| α-helix | 19-29 | 11 | |
| 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 | 82-90 | 9 | |
| 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 | 169-184 | 16 | |
| β-strand | 190-194 | 5 | 3 |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-8 | 2 | |
Molecules and chains
| 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 | |
Sequence of entity 1 (A, C), FASTA
>4IMI_1 Symplekin (chains A, C)
GPGSGMTDEKTATARAKVVDWCNELVIASPSTKCELLAKVQETVLGSCAELAEEFLESVL
SLAHDSNMEVRKQVVAFVEQVCKVKVELLPHVINVVSMLLRDNSAQVIKRVIQACGSIYK
NGLQYLCSLMEPGDSAEQAWNILSLIKAQILDMIDNENDGIRTNAIKFLEGVVVLQSFAD
EDSLKRDGDFSLADVPDHCTLFRREKLQEEGNNILDILLQFHGTTHISSVNLIACTSSLC
TIAKMRPIFMGAVVEAFKQLNANLPPTLTDSQVSSVRKSLKMQLQTLLKNRGAFEFASTI
RGMLVDLGSSTNEIQKLIPKMDKQEMARRQKRILENAAQ
Sequence of entity 2 (B, D), FASTA
>4IMI_2 CG14216 (chains B, D)
GPGSGMTDPSKLAVAVVDSSNMNRSMEAHNFLAKKGFNVRSYGTGERVKLPGMAFDKPNV
YEFGTKYEDIYRDLESKDKEFYTQNGLLHMLDRNRRIKKCPERFQDTKEQFDIIVTVEER
VYDLVVMHMESMESVDNRPVHVLNVDVVNNAEDALMGAFVITDMINMMAKSTDLDNDIDE
LIQEFEERRKRVILHSVLFY
Sequence of entity 3 (F), FASTA
>4IMI_3 CTD (chains F)
SPSYSPTSPSYSPTSPSYS
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| PO4 | Phosphate ion | O4 P | 1 |
Primary citation
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:
- 3GS3 2.4 Å, Structure of the N-terminal HEAT Domain of Symplekin from D. melanogaster
- 6NPW 2.49 Å, SSu72/Sympk in complex with Ser2/Ser5 phosphorylated peptide
- 4IMJ 2.58 Å, Novel Modifications on C-terminal Domain of RNA Polymerase II can Fine-tune the…
- 4YGX 2.95 Å, Crystal Structure of D. melanogaster Ssu72+Symplekin bound to cis peptidomimetic CTD…
Browse structure collections
About this viewer
MolViewer shows 4IMI directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.