Research workbench
Crystal structure of a highly specific aspergillus ribotoxin, restrictocin
Analyse Crystal structure of a highly specific aspergillus ribotoxin, restrictocin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AQZ
- Type
- protein
- Length
- 285 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Restrictocin
- EC
- 3.1.27.-
- UniProt
- P67876
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Restrictocin (EC 3.1.27.-) | protein | 142 | 10% helix, 32% strand | P67876 |
| B | Restrictocin (EC 3.1.27.-) | protein | 143 | 10% helix, 36% strand | P67876 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 295 | 0.62 | 0.79 | 43 | empty |
| 2 | 51 | 0.43 | 0.84 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 238 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1AQZ · Crystal structure of a highly specific aspergillus ribotoxin, restrictocin · the same entry in another collection · chain A against A, TM-score 1.00
- P67876 · AlphaFold monomer V2.0 prediction for ribonuclease mitogillin (P67876) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P67876
- Elsewhere: RCSB PDB 1AQZ · PDBe 1AQZ · UniProt P67876
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