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Crystal structure of N-terminal human IFIT1
Analyse Crystal structure of N-terminal human IFIT1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HOU
- Type
- protein
- Length
- 503 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interferon-induced protein with tetratricopeptide repeats 1
- UniProt
- P09914
- Pockets
- 7 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interferon-induced protein with tetratricopeptide repeats 1 | protein | 261 | 72% helix, 0% strand | P09914 |
| B | Interferon-induced protein with tetratricopeptide repeats 1 | protein | 242 | 73% helix, 0% strand | P09914 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 373 | 0.61 | 0.77 | 39 | empty |
| 2 | 163 | 0.50 | 0.78 | 38 | empty |
| 3 | 191 | 0.49 | 0.76 | 21 | empty |
| 4 | 107 | 0.44 | 0.78 | 16 | empty |
| 5 | 59 | 0.34 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 461 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 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 P09914
- Elsewhere: RCSB PDB 4HOU · PDBe 4HOU · UniProt P09914
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