Research workbench
Structure of the leukemia inhibitory factor receptor (lif-R) domains D1-D5
Analyse Structure of the leukemia inhibitory factor receptor (lif-R) domains D1-D5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E0G
- Type
- protein
- Length
- 479 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leukemia inhibitory factor receptor
- UniProt
- P42702
- Ligands
- NAG, FUC, MAN
- Pockets
- 5 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leukemia inhibitory factor receptor | protein | 479 | 3% helix, 41% strand | P42702 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A
- MAN · alpha-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.65 | 0.93 | 21 | empty |
| 2 | 104 | 0.59 | 0.86 | 21 | empty |
| 3 | 124 | 0.47 | 0.78 | 23 | empty |
| 4 | 62 | 0.33 | 0.76 | 15 | empty |
| 5 | 60 | 0.29 | 0.74 | 22 | empty |
Modifications
Observed in the structure: 5 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 3E0G · Structure of the Leukemia Inhibitory Factor Receptor (LIF-R) domains D1-D5 · the same entry in another collection · chain A against A, TM-score 1.00
- P42702 · AlphaFold monomer V2.0 prediction for leukemia inhibitory factor receptor (P42702) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P42702
- Elsewhere: RCSB PDB 3E0G · PDBe 3E0G · UniProt P42702
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