Research workbench
Crystal Structure of Full-Length Human IFIT5 with 5`-triphosphate Oligocytidine
Analyse Crystal Structure of Full-Length Human IFIT5 with 5`-triphosphate Oligocytidine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HOR
- Type
- protein + RNA
- Length
- 486 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.861
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- Molecule
- Interferon-induced protein with tetratricopeptide repeats 5; RNA…
- UniProt
- Q13325
- Ligands
- MG
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · resolution 1.861 · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interferon-induced protein with tetratricopeptide repeats 5 | protein | 482 | 77% helix, 0% strand | Q13325 |
| X | RNA (5'-R(*(CTP)P*CP*CP*CP*C)-3') | rna | 4 | — | — |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A, X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 496 | 0.67 | 0.79 | 54 | empty |
| 2 | 176 | 0.63 | 0.84 | 38 | empty |
Interfaces
1 interface between chains.
- A–X · 883 Ų buried · 32 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 modified (nucleotide modification).
Compared structures
- 4HOR · Crystal structure of full-length human IFIT5 with 5`-triphosphate oligocytidine · the same entry in another collection · chain A against A, TM-score 1.00
- Q13325 · AlphaFold monomer V2.0 prediction for interferon-induced protein with tetratricopeptide… · a predicted model of the same protein · chain A 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 Q13325
- Elsewhere: RCSB PDB 4HOR · PDBe 4HOR · UniProt Q13325
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.