MolNFT v1 · #94179 · protein + RNA
Crystal structure of full-length human IFIT5 with 5`-triphosphate oligocytidine
4HOR · Interferon-induced protein with tetratricopeptide repeats 5: “Crystal structure of full-length human IFIT5 with 5`-triphosphate oligocytidine”. X-ray diffraction, 1 ligand (MG), 2 pockets (best druggability 0.67). MolNFT v1 #94179…
- PDB
- 4HOR
- Type
- protein + RNA
- Length
- 486 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interferon-induced protein with tetratricopeptide repeats 5; RNA…
- UniProt
- Q13325
- Ligands
- MG
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 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
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