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Crystal structure of full-length human IFIT5
Analyse Crystal structure of full-length human IFIT5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HOQ
- Type
- protein
- Length
- 477 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interferon-induced protein with tetratricopeptide repeats 5
- UniProt
- Q13325
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interferon-induced protein with tetratricopeptide repeats 5 | protein | 477 | 76% helix, 0% strand | Q13325 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 754 | 0.72 | 0.78 | 52 | empty |
| 2 | 233 | 0.65 | 0.83 | 34 | empty |
| 3 | 52 | 0.31 | 0.77 | 11 | empty |
| 4 | 50 | 0.28 | 0.75 | 13 | empty |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
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 4HOQ · PDBe 4HOQ · UniProt Q13325
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