MolNFT v2 · #1566 · protein
Ovine interferon tau
1B5L: “Ovine interferon tau”. X-ray diffraction at 2.1, 1 ligand (SO4), 1 pocket (best druggability 0.38). MolNFT v2 #1566 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1B5L
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Pichia pastoris
- Molecule
- Interferon tau
- UniProt
- P56828
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interferon tau | protein | 152 | 74% helix, 0% strand | P56828 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.38 | 0.76 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P56828
- Elsewhere: RCSB PDB 1B5L · PDBe 1B5L · UniProt P56828
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