Crystal structure of the D1D2 sub-complex from the human snrnp core domain. Determined by X-ray diffraction at 2.5 Å resolution. Released 13 Jan 2000.
Explore 1B34 in 3D Show helices and sheets RCSB PDB PDBe
1B34 contains 5 α-helices and 10 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 | 3-8 | 6 | |
| β-strand | 14-19 | 6 | 1 |
| β-strand | 24-32 | 9 | 1 |
| β-strand | 38-46 | 9 | 1 |
| β-strand | 53-60 | 8 | 1 |
| α-helix | 62-64 | 3 | |
| β-strand | 65-69 | 5 | 1 |
| α-helix | 76-79 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-38 | 11 | |
| β-strand | 41-46 | 6 | 1 |
| β-strand | 51-59 | 9 | 1 |
| β-strand | 65-72 | 8 | 1 |
| β-strand | 94-101 | 8 | 1 |
| α-helix | 103-105 | 3 | |
| β-strand | 106-111 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (small nuclear ribonucleoprotein sm D1) | A | protein | 119 | Homo sapiens | P62314 (AlphaFold model) |
| Protein (small nuclear ribonucleoprotein sm D2) | B | protein | 118 | Homo sapiens | P62316 (AlphaFold model) |
>1B34_1 PROTEIN (SMALL NUCLEAR RIBONUCLEOPROTEIN SM D1) (chains A) MKLVRFLMKLSHETVTIELKNGTQVHGTITGVDVSMNTHLKAVKMTLKNREPVQLETLSI RGNNIRYFILPDSLPLDTLLVDVEPKVKSKKREAVAGRGRGRGRGRGRGRGRGRGGPRR
>1B34_2 PROTEIN (SMALL NUCLEAR RIBONUCLEOPROTEIN SM D2) (chains B) MSLLNKPKSEMTPEELQKREEEEFNTGPLSVLTQSVKNNTQVLINCRNNKKLLGRVKAFD RHCNMVLENVKEMWTEVPKSGKGKKKSKPVNKDRYISKMFLRGDSVIVVLRNPLIAGK
Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Kambach, C., Walke, S., Young, R. et al. Cell (1999) 96:375-387. DOI 10.1016/S0092-8674(00)80550-4 · PubMed
Other PDB entries of the same protein (UniProt P62314 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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