human RPRD1B CID in complex with a RPB1-CTD derived Ser2 phosphorylated peptide. Determined by X-ray diffraction at 1.85 Å resolution. Released 18 Jun 2014.
Explore 4Q94 in 3D Show helices and sheets RCSB PDB PDBe
4Q94 contains 19 α-helices and 4 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 | 6-15 | 10 | |
| β-strand | 19 | 1 | 1 |
| α-helix | 20-32 | 13 | |
| α-helix | 34-36 | 3 | |
| α-helix | 37-50 | 14 | |
| α-helix | 53-55 | 3 | |
| α-helix | 56-70 | 15 | |
| α-helix | 76-82 | 7 | |
| α-helix | 85-113 | 29 | |
| α-helix | 119-129 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-15 | 10 | |
| β-strand | 19 | 1 | 2 |
| α-helix | 20-32 | 13 | |
| α-helix | 34-36 | 3 | |
| α-helix | 37-50 | 14 | |
| α-helix | 53-55 | 3 | |
| α-helix | 56-70 | 15 | |
| α-helix | 76-113 | 38 | |
| α-helix | 119-128 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1620 | 1 | |
| β-strand | 1621 | 1 | 1 |
| α-helix | 1622 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1621 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulation of nuclear pre-mRNA domain-containing protein 1B | A, B | protein | 135 | Homo sapiens | Q9NQG5 (AlphaFold model) |
| rpb1-ctd | C, D | protein | 21 |
>4Q94_1 Regulation of nuclear pre-mRNA domain-containing protein 1B (chains A, B) GSSFSESALEKKLSELSNSQHSVQTLSLWLIHHRKHAGPIVSVWHRELRKAKSNRKLTFL YLANDVIQNSKRKGPEFTREFESVLVDAFSHVAREADEGCKKPLERLLNIWQERSVYGGE FIQQLKLSMEDSKSP
>4Q94_2 rpb1-ctd (chains C, D) XSPSYSPTSPSYSPTSPSYSX
RPRD1A and RPRD1B are human RNA polymerase II C-terminal domain scaffolds for Ser5 dephosphorylation. Ni, Z., Xu, C., Guo, X. et al. Nat Struct Mol Biol (2014) 21:686-695. DOI 10.1038/nsmb.2853 · PubMed
Other PDB entries of the same protein (UniProt Q9NQG5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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