MolNFT v1 · #76681 · protein
Crystal structure of a human FLT3 ligand-receptor ternary complex
3QS7 · Sl cytokine: “Crystal structure of a human FLT3 ligand-receptor ternary complex”. X-ray diffraction, 1 ligand (NAG), 19 pockets (best druggability 0.65). MolNFT v1 #76681 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3QS7
- Type
- protein
- Length
- 1,627 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sl cytokine; Fl cytokine receptor
- EC
- 2.7.10.1
- UniProt
- P49771, P36888
- Ligands
- NAG
- Pockets
- 19 · best druggability 0.65
Structure
x-ray diffraction · 7 distinct chains · 14% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Sl cytokine | protein | 135 | 48% helix, 9% strand | P49771 |
| B | Sl cytokine | protein | 134 | 48% helix, 10% strand | P49771 |
| D | Sl cytokine | protein | 132 | 49% helix, 11% strand | P49771 |
| E | Fl cytokine receptor (EC 2.7.10.1) | protein | 328 | 1% helix, 57% strand | P36888 |
| F | Fl cytokine receptor (EC 2.7.10.1) | protein | 336 | 2% helix, 56% strand | P36888 |
| G | Fl cytokine receptor (EC 2.7.10.1) | protein | 168 | 2% helix, 57% strand | P36888 |
| H | Fl cytokine receptor (EC 2.7.10.1) | protein | 259 | 2% helix, 55% strand | P36888 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 553 | 0.65 | 0.76 | 53 | empty |
| 2 | 519 | 0.63 | 0.75 | 56 | empty |
| 3 | 528 | 0.63 | 0.75 | 47 | empty |
| 4 | 455 | 0.62 | 0.76 | 40 | empty |
| 5 | 257 | 0.57 | 0.78 | 37 | empty |
Interfaces
10 interfaces between chains.
- A–B · 758 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 753 Ų buried · 13 hydrogen bonds · protein-protein
- A–E · 511 Ų buried · 10 hydrogen bonds · protein-protein
- B–F · 511 Ų buried · 8 hydrogen bonds · protein-protein
- C–G · 510 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 disulfide, 7 glycan (disulfide, N-glycosylation).
Compared structures
- 3QS7 · Crystal structure of a human Flt3 ligand-receptor ternary complex · the same entry in another collection · chain H against H, TM-score 1.00
- P49771 · AlphaFold monomer V2.0 prediction for fms-related tyrosine kinase 3 ligand (P49771) · a predicted model of the same protein · chain D against A, TM-score 1.00
- P36888 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein kinase FLT3 (P36888) · a predicted model of the same protein · chain G against A, TM-score 0.98
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 P49771
- Every structure of UniProt P36888
- Elsewhere: RCSB PDB 3QS7 · PDBe 3QS7 · UniProt P49771 · UniProt P36888
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