Structure, phosphorylation and U2AF65 binding of the Nterminal Domain of splicing factor 1 during 3 splice site Recognition. Determined by solution NMR. Released 30 Jan 2013.
Explore 2M0G in 3D Show helices and sheets RCSB PDB PDBe
2M0G contains 6 α-helices and 4 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 |
|---|---|---|---|
| α-helix | 39-41 | 3 | |
| α-helix | 46-67 | 22 | |
| α-helix | 97-119 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 377-381 | 5 | 1 |
| α-helix | 392-406 | 15 | |
| β-strand | 412-416 | 5 | 1 |
| β-strand | 431-436 | 6 | 1 |
| α-helix | 439-449 | 11 | |
| β-strand | 460-464 | 5 | 1 |
| α-helix | 466-470 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Splicing factor 1 | A | protein | 145 | Homo sapiens | Q15637 (AlphaFold model) |
| Splicing factor U2AF 65 kDa subunit | B | protein | 104 | Homo sapiens | P26368 (AlphaFold model) |
>2M0G_1 Splicing factor 1 (chains A) MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIED LTRKLRTGDLGIPPNPEDRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHNLITEMVALN PDFKPPADYKPPATRVCDKVMIPQD
>2M0G_2 Splicing factor U2AF 65 kDa subunit (chains B) GHPTEVLCLMNMVLPEELLDDEEYEEIVEDVRDECSKYGLVKSIEIPRPVDGVEVPGCGK IFVEFTSVFDCQKAMQGLTGRKFANRVVVTKYCDPDSYHRRDFW
Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition. Zhang, Y., Madl, T., Bagdiul, I. et al. Nucleic Acids Res (2013) 41:1343-1354. DOI 10.1093/nar/gks1097 · PubMed
Other PDB entries of the same protein (UniProt Q15637 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2M0G 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.