Research workbench
Crystal structure of ISG15, the interferon-induced ubiquitin cross reactive protein
Analyse Crystal structure of ISG15, the interferon-induced ubiquitin cross reactive… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z2M
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interferon, alpha-inducible protein (clone ifi-15K)
- UniProt
- P05161
- Ligands
- OS4
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interferon, alpha-inducible protein (clone ifi-15K) | protein | 152 | 24% helix, 34% strand | P05161 |
Ligands and binding sites
- OS4 · Osmium 4+ ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1Z2M · Crystal Structure of ISG15, the Interferon-Induced Ubiquitin Cross Reactive Protein · the same entry in another collection · chain A against A, TM-score 1.00
- P05161 · AlphaFold monomer V2.0 prediction for ubiquitin-like protein ISG15 (P05161) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P05161
- Elsewhere: RCSB PDB 1Z2M · PDBe 1Z2M · UniProt P05161
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