Human raver1 RRM1-3 domains (residues 39-320). Determined by X-ray diffraction at 1.99 Å resolution. Released 10 Aug 2011.
Explore 3SMZ in 3D Show helices and sheets RCSB PDB PDBe
3SMZ contains 15 α-helices and 18 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 | 38-40 | 3 | |
| α-helix | 41-56 | 16 | |
| β-strand | 60-64 | 5 | 1 |
| α-helix | 72-78 | 7 | |
| β-strand | 84-90 | 7 | 1 |
| β-strand | 95-100 | 6 | 1 |
| α-helix | 103-113 | 11 | |
| β-strand | 117-118 | 2 | 2 |
| β-strand | 121-122 | 2 | 2 |
| α-helix | 123 | 1 | |
| β-strand | 124-127 | 4 | 1 |
| α-helix | 128-129 | 2 | |
| β-strand | 133-137 | 5 | 3 |
| α-helix | 145-152 | 8 | |
| α-helix | 153-155 | 3 | |
| β-strand | 158-165 | 8 | 3 |
| β-strand | 172-180 | 9 | 3 |
| α-helix | 183-193 | 11 | |
| β-strand | 197-198 | 2 | 4 |
| β-strand | 201-202 | 2 | 4 |
| β-strand | 204-207 | 4 | 3 |
| α-helix | 210-212 | 3 | |
| β-strand | 222-226 | 5 | 5 |
| α-helix | 228-229 | 2 | |
| α-helix | 235-241 | 7 | |
| β-strand | 250-255 | 6 | 5 |
| β-strand | 261-268 | 8 | 5 |
| α-helix | 272-282 | 11 | |
| β-strand | 286-287 | 2 | 6 |
| β-strand | 290-291 | 2 | 6 |
| β-strand | 293-296 | 4 | 5 |
| α-helix | 297-298 | 2 | |
| α-helix | 303-313 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ribonucleoprotein PTB-binding 1 | A | protein | 284 | Homo sapiens | Q8IY67 (AlphaFold model) |
>3SMZ_1 Ribonucleoprotein PTB-binding 1 (chains A) HMLDPEEIRKRLEHTERQFRNRRKILIRGLPGDVTNQEVHDLLSDYELKYCFVDKYKGTA FVTLLNGEQAEAAINAFHQSRLRERELSVQLQPTDALLCVANLPPSLTQQQFEELVRPFG SLERCFLVYSERTGQSKGYGFAEYMKKDSAARAKSDLLGKPLGPRTLYVHWTDAGQLTPA LLHSRCLCVDRLPPGFNDVDALCRALSAVHSPTFCQLACGQDGQLKGFAVLEYETAEMAE EAQQQADGLSLGGSHLRVSFCAPGPPGRSMLAALIAAQATALNR
Apo raver1 structure reveals distinct RRM domain orientations. Rangarajan, E.S., Lee, J.H., Izard, T. Protein Sci (2011) 20:1464-1470. DOI 10.1002/pro.664 · PubMed
Other PDB entries of the same protein (UniProt Q8IY67 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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