Research workbench
Crystal structure of the isolated E. COLI rele toxin, P21 form
Analyse Crystal structure of the isolated E. COLI rele toxin, P21 form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FXI
- Type
- protein
- Length
- 282 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MRNA interferase rele
- EC
- 3.1.-.-
- UniProt
- P0C077
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | MRNA interferase rele (EC 3.1.-.-) | protein | 94 | 47% helix, 29% strand | P0C077 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B, C
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 | 1086 | 0.72 | 0.76 | 67 | SO4 |
| 2 | 60 | 0.28 | 0.73 | 12 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1267 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 400 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 158 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (artifact).
Compared structures
- 4FXI · Crystal structure of the isolated E. coli RelE toxin, P21 form · the same entry in another collection · chain A against A, TM-score 1.00
- P0C077 · AlphaFold monomer V2.0 prediction for mRNA interferase toxin rele (P0C077) · 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 P0C077
- Elsewhere: RCSB PDB 4FXI · PDBe 4FXI · UniProt P0C077
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