Research workbench
Crystal structure of leukemia inhibitory factor in complex with lif receptor (domains 1-5)
Analyse Crystal structure of leukemia inhibitory factor in complex with lif receptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q7N
- Type
- protein
- Length
- 1,320 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leukemia inhibitory factor receptor; Leukemia inhibitory factor
- UniProt
- P42703, P15018
- Ligands
- NAG, FUC, MAN
- Pockets
- 10 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Leukemia inhibitory factor receptor | protein | 480 | 1% helix, 45% strand | P42703 |
| B, D | Leukemia inhibitory factor | protein | 180 | 59% helix, 0% strand | P15018 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 33 copies · chains A, D, C
- FUC · alpha-L-fucopyranose · sugar · 7 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 5 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 481 | 0.82 | 0.89 | 62 | empty |
| 2 | 499 | 0.68 | 0.79 | 52 | empty |
| 3 | 477 | 0.66 | 0.78 | 47 | empty |
| 4 | 97 | 0.47 | 0.81 | 16 | empty |
| 5 | 66 | 0.37 | 0.78 | 24 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1423 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 1029 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1001 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 430 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 397 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 18 glycan, 16 disulfide (N-glycosylation, disulfide).
Compared structures
- 2Q7N · Crystal structure of Leukemia inhibitory factor in complex with LIF receptor (domains 1-5) · the same entry in another collection · chain A against A, TM-score 1.00
- P42703 · AlphaFold monomer V2.0 prediction for leukemia inhibitory factor receptor (P42703) · a predicted model of the same protein · chain A against A, TM-score 0.94
- P15018 · AlphaFold monomer V2.0 prediction for leukemia inhibitory factor (P15018) · a predicted model of the same protein · chain B against A, TM-score 0.90
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 P42703
- Every structure of UniProt P15018
- Elsewhere: RCSB PDB 2Q7N · PDBe 2Q7N · UniProt P42703 · UniProt P15018
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