Research workbench
ASP79 makes a large, unfavorable contribution to the stability of RNase sa
Analyse ASP79 makes a large, unfavorable contribution to the stability of RNase sa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YNV
- Type
- protein
- Length
- 96 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanyl-specific ribonuclease sa
- EC
- 3.1.27.3
- UniProt
- P05798
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Guanyl-specific ribonuclease sa (EC 3.1.27.3) | protein | 96 | 15% helix, 21% strand | P05798 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1YNV · Asp79 makes a large, unfavorable contribution to the stability of RNase Sa · the same entry in another collection · chain X against X, TM-score 1.00
- P05798 · AlphaFold monomer V2.0 prediction for guanyl-specific ribonuclease sa (P05798) · a predicted model of the same protein · chain X against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P05798
- Elsewhere: RCSB PDB 1YNV · PDBe 1YNV · UniProt P05798
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