yeast NOT1 CN9BD-CAF40 complex. Determined by X-ray diffraction at 3.81 Å resolution. Released 7 May 2014.
Explore 4CV5 in 3D Show helices and sheets RCSB PDB PDBe
4CV5 contains 56 α-helices and 0 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 | 1073-1076 | 4 | |
| α-helix | 1081-1083 | 3 | |
| α-helix | 1086-1126 | 41 | |
| α-helix | 1133-1170 | 38 | |
| α-helix | 1186-1216 | 31 | |
| α-helix | 1218-1229 | 12 | |
| α-helix | 1262-1267 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 108-116 | 9 | |
| α-helix | 122-130 | 9 | |
| α-helix | 139-144 | 6 | |
| α-helix | 148-157 | 10 | |
| α-helix | 161-163 | 3 | |
| α-helix | 171-186 | 16 | |
| α-helix | 190-198 | 9 | |
| α-helix | 202-204 | 3 | |
| α-helix | 206-209 | 4 | |
| α-helix | 216-232 | 17 | |
| α-helix | 238-244 | 7 | |
| α-helix | 249-258 | 10 | |
| α-helix | 262-277 | 16 | |
| α-helix | 281-284 | 4 | |
| α-helix | 289-305 | 17 | |
| α-helix | 314-326 | 13 | |
| α-helix | 330-339 | 10 | |
| α-helix | 342-345 | 4 | |
| α-helix | 350-353 | 4 | |
| α-helix | 357-369 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1073-1076 | 4 | |
| α-helix | 1081-1083 | 3 | |
| α-helix | 1086-1126 | 41 | |
| α-helix | 1133-1170 | 38 | |
| α-helix | 1186-1216 | 31 | |
| α-helix | 1218-1230 | 13 | |
| α-helix | 1235-1236 | 2 | |
| α-helix | 1244-1246 | 3 | |
| α-helix | 1262-1269 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 108-116 | 9 | |
| α-helix | 122-130 | 9 | |
| α-helix | 139-144 | 6 | |
| α-helix | 148-157 | 10 | |
| α-helix | 161-163 | 3 | |
| α-helix | 170-188 | 19 | |
| α-helix | 190-198 | 9 | |
| α-helix | 201-204 | 4 | |
| α-helix | 206-209 | 4 | |
| α-helix | 216-232 | 17 | |
| α-helix | 238-246 | 9 | |
| α-helix | 249-258 | 10 | |
| α-helix | 262-277 | 16 | |
| α-helix | 281-284 | 4 | |
| α-helix | 289-304 | 16 | |
| α-helix | 315-326 | 12 | |
| α-helix | 330-339 | 10 | |
| α-helix | 342-345 | 4 | |
| α-helix | 350-353 | 4 | |
| α-helix | 357-369 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| General negative regulator of transcription subunit 1 | A, C | protein | 212 | SACCHAROMYCES CEREVISIAE | P25655 (AlphaFold model) |
| Protein CAF40 | B, D | protein | 320 | SACCHAROMYCES CEREVISIAE | P53829 (AlphaFold model) |
>4CV5_1 GENERAL NEGATIVE REGULATOR OF TRANSCRIPTION SUBUNIT 1 (chains A, C) NPFNNLLGSTIFVTHPDLKRVFQMALAKSVREILLEVVEKSSGIAVVTTTKIILKDFATE VDESKLKTAAIIMVRHLAQSLARATSIEPLKEGIRSTMQSLAPNLMSLSSSPAEELDTAI NENIGIALVLIEKASMDKSTQDLADQLMQAIAIRRYHKERRADQPFITQNTNPYSLSLPE PLGLKNTGVTPQQFRVYEEFGKNIPNLDVIPF
>4CV5_2 PROTEIN CAF40 (chains B, D) LMGNTPNNNNSNENGENNGNNGNNGGNDANATRNNPNMVNNRGAVHALDDPNVYHWICQL TYGPQKEQALLELGRKREQFDDLAVVLWSSFGVMTSLLNEIISVYPMLQPQMLSNNLSNR VCNALVLLQCVASHPETKHLFLQAHIPLFLFPFLNTTSRQRTFEYLRLTSLGVIGALVKN DSQDVITFLLRTDIVPLCLRIMESSSELSKTVAIFILQKILLDDVGLQYICATLERFYAV TNVLKDMVEHLTVSTPPGRLLKHIIRCYLRLSDDLEARRLLKIVLPAKLRDNTFTEVLRD DVGSKRCLAQLLLTLNEETS
| ID | Name | Formula | Copies |
|---|---|---|---|
| TBR | Hexatantalum dodecabromide | Br12 Ta6 | 3 |
Structural and Biochemical Insights to the Role of the Ccr4-not Complex and Ddx6 ATPase in Microrna Repression. Mathys, H., Basquin, J., Ozgur, S. et al. Mol Cell (2014) 54:751. DOI 10.1016/J.MOLCEL.2014.03.036 · PubMed
Other PDB entries of the same protein (UniProt P25655 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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