Research workbench
Cytokyne-binding region of GP130
Analyse Cytokyne-binding region of GP130 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BQU
- Type
- protein
- Length
- 423 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (GP130)
- UniProt
- P40189
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (GP130) | protein | 208 | 9% helix, 43% strand | P40189 |
| B | Protein (GP130) | protein | 215 | 8% helix, 40% strand | P40189 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.43 | 0.75 | 21 | empty |
| 2 | 102 | 0.34 | 0.73 | 18 | SO4 |
Interfaces
1 interface between chains.
- A–B · 480 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 P40189
- Elsewhere: RCSB PDB 1BQU · PDBe 1BQU · UniProt P40189
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