Research workbench
Crystal structure of RNase SA3, cytotoxic microbial ribonuclease
Analyse Crystal structure of RNase SA3, cytotoxic microbial ribonuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MGW
- Type
- protein
- Length
- 99 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanyl-specific ribonuclease SA3
- EC
- 3.1.27.3
- UniProt
- P30289
- Ligands
- LI
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanyl-specific ribonuclease SA3 (EC 3.1.27.3) | protein | 99 | 15% helix, 20% strand | P30289 |
Ligands and binding sites
- LI · Lithium ion · metal · chains A
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
- 1MGW · Crystal structure of RNase Sa3, cytotoxic microbial ribonuclease · the same entry in another collection · chain A against A, TM-score 1.00
- P30289 · AlphaFold monomer V2.0 prediction for guanyl-specific ribonuclease SA3 (P30289) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P30289
- Elsewhere: RCSB PDB 1MGW · PDBe 1MGW · UniProt P30289
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