Research workbench
Crystal structure of the second hin-200 domain of interferon-inducible protein 16
Analyse Crystal structure of the second hin-200 domain of interferon-inducible protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B6Y
- Type
- protein
- Length
- 369 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-interferon-inducible protein ifi-16
- UniProt
- Q16666
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-interferon-inducible protein ifi-16 | protein | 185 | 12% helix, 49% strand | Q16666 |
| B | Gamma-interferon-inducible protein ifi-16 | protein | 184 | 13% helix, 51% strand | Q16666 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 255 | 0.54 | 0.77 | 35 | empty |
| 2 | 231 | 0.50 | 0.75 | 31 | empty |
| 3 | 65 | 0.27 | 0.73 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 62 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3B6Y · Crystal Structure of the Second HIN-200 Domain of Interferon-Inducible Protein 16 · the same entry in another collection · chain A against A, TM-score 1.00
- Q16666 · AlphaFold monomer V2.0 prediction for gamma-interferon-inducible protein 16 (Q16666) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q16666
- Elsewhere: RCSB PDB 3B6Y · PDBe 3B6Y · UniProt Q16666
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