Asp79 makes a large, unfavorable contribution to the stability of RNase Sa. Determined by X-ray diffraction at 1.2 Å resolution. Released 19 Jul 2005.
Explore 1YNV in 3D Show helices and sheets RCSB PDB PDBe
1YNV contains 6 α-helices and 6 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 |
|---|---|---|---|
| β-strand | 5-7 | 3 | 1 |
| α-helix | 8-10 | 3 | |
| α-helix | 13-23 | 11 | |
| α-helix | 35 | 1 | |
| β-strand | 36 | 1 | 1 |
| α-helix | 37 | 1 | |
| α-helix | 45-46 | 2 | |
| β-strand | 53-56 | 4 | 1 |
| α-helix | 58-59 | 2 | |
| β-strand | 69-72 | 4 | 1 |
| β-strand | 79-82 | 4 | 1 |
| β-strand | 90-93 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanyl-specific ribonuclease Sa | X | protein | 96 | Streptomyces aureofaciens | P05798 (AlphaFold model) |
>1YNV_1 Guanyl-specific ribonuclease Sa (chains X) DVSGTVCLSALPPEATDTLNLIASDGPFPYSQDGVVFQNRESVLPTQSYGYYHEYTVITP GARTRGTRRIITGEATQEDYYTGDHYATFSLIDKTC
Asp79 Makes a Large, Unfavorable Contribution to the Stability of RNase Sa. Trevino, S.R., Gokulan, K., Newsom, S. et al. J Mol Biol (2005) 354:967-978. DOI 10.1016/j.jmb.2005.09.091 · PubMed
Other PDB entries of the same protein (UniProt P05798 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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