Three-dimensional structure of a RNA-polymerase II binding protein. Determined by X-ray diffraction at 2.3 Å resolution. Released 31 Aug 2004.
Explore 1T9Z in 3D Show helices and sheets RCSB PDB PDBe
1T9Z contains 13 α-helices and 11 β-strands across 1 chain. 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 | 82-84 | 3 | |
| α-helix | 85-87 | 3 | |
| α-helix | 91 | 1 | |
| β-strand | 92-95 | 4 | 1 |
| β-strand | 98 | 1 | 2 |
| β-strand | 102-105 | 4 | 2 |
| β-strand | 114-120 | 7 | 2 |
| β-strand | 123-131 | 9 | 2 |
| α-helix | 132 | 1 | |
| α-helix | 135-145 | 11 | |
| β-strand | 147-151 | 5 | 1 |
| α-helix | 156-166 | 11 | |
| β-strand | 172-176 | 5 | 1 |
| α-helix | 178-180 | 3 | |
| β-strand | 182-184 | 3 | 3 |
| β-strand | 187-189 | 3 | 3 |
| α-helix | 192-194 | 3 | |
| α-helix | 199-201 | 3 | |
| β-strand | 202-205 | 4 | 1 |
| α-helix | 209-212 | 4 | |
| α-helix | 216-218 | 3 | |
| β-strand | 219 | 1 | 1 |
| α-helix | 233-244 | 12 | |
| α-helix | 250-254 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 | A | protein | 197 | Homo sapiens | Q9GZU7 (AlphaFold model) |
>1T9Z_1 Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 (chains A) MQYLLPEAKAQDSDKICVVIDLDETLVHSSFKPVNNADFIIPVEIDGVVHQVYVLKRPHV DEFLQRMGELFECVLFTASLAKYADPVADMLDKWGAFRARLFRESCVFHRGNYVKDLSRL GRDLRRVLIMDNSPASYVFHPDNAVPVASWFDNMSDTELHDLLPFFEQLSRVDDVYSVLR QPRPGSAAALEHHHHHH
Structure and Mechanism of RNA Polymerase II CTD Phosphatases. Kamenski, T., Heilmeier, S., Meinhart, A. et al. Mol Cell (2004) 15:399-407. DOI 10.1016/j.molcel.2004.06.035 · PubMed
Other PDB entries of the same protein (UniProt Q9GZU7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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