Crystal structure of human PHF5A. Determined by X-ray diffraction at 1.82 Å resolution. Released 7 Sept 2016.
Explore 5SYB in 3D Show helices and sheets RCSB PDB PDBe
5SYB contains 16 α-helices and 22 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 8-10 | 3 | 1 |
| α-helix | 13-15 | 3 | |
| β-strand | 18-19 | 2 | 2 |
| α-helix | 20 | 1 | |
| β-strand | 21-22 | 2 | 3 |
| α-helix | 38 | 1 | |
| β-strand | 39-42 | 4 | 4 |
| β-strand | 44-45 | 2 | 2 |
| α-helix | 47-50 | 4 | |
| β-strand | 57 | 1 | 5 |
| β-strand | 58 | 1 | 3 |
| α-helix | 63 | 1 | |
| β-strand | 64 | 1 | 5 |
| α-helix | 65 | 1 | |
| β-strand | 67-68 | 2 | 3 |
| β-strand | 70-72 | 3 | 4 |
| α-helix | 73-77 | 5 | |
| α-helix | 80-83 | 4 | |
| β-strand | 88-90 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-10 | 3 | 6 |
| α-helix | 13-15 | 3 | |
| β-strand | 18-19 | 2 | 7 |
| α-helix | 20 | 1 | |
| β-strand | 21-22 | 2 | 8 |
| α-helix | 37-38 | 2 | |
| β-strand | 39-42 | 4 | 9 |
| β-strand | 44-45 | 2 | 7 |
| α-helix | 52-54 | 3 | |
| β-strand | 57 | 1 | 10 |
| β-strand | 58 | 1 | 8 |
| α-helix | 63 | 1 | |
| β-strand | 64 | 1 | 10 |
| α-helix | 65 | 1 | |
| β-strand | 67-68 | 2 | 8 |
| β-strand | 70-72 | 3 | 9 |
| α-helix | 73-77 | 5 | |
| α-helix | 80-83 | 4 | |
| β-strand | 88-90 | 3 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| PHD finger-like domain-containing protein 5A | A, B | protein | 113 | Homo sapiens | Q7RTV0 (AlphaFold model) |
>5SYB_1 PHD finger-like domain-containing protein 5A (chains A, B) GGHMAKHHPDLIFCRKQAGVAIGRLCEKCDGKCVICDSYVRPSTLVRICDECNYGSYQGR CVICGGPGVSDAYYCKECTIQEKDRDGCPKIVNLGSSKTDLFYERKKYGFKKR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 6 |
Water and common crystallization additives (EDO) are not listed.
Splicing modulators act at the branch point adenosine binding pocket defined by the PHF5A-SF3b complex. Teng, T., Tsai, J.H., Puyang, X. et al. Nat Commun (2017) 8:15522-15522. DOI 10.1038/ncomms15522 · PubMed
Other PDB entries of the same protein (UniProt Q7RTV0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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