Research workbench
FGFR3 in complex with a Fab
Analyse FGFR3 in complex with a Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GRW
- Type
- protein
- Length
- 650 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibroblast growth factor receptor 3; Fab light chain; Fab heavy chain
- UniProt
- Q8NI16
- Ligands
- NAG, SO4
- Pockets
- 7 · best druggability 0.56
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibroblast growth factor receptor 3 | protein | 206 | 8% helix, 51% strand | Q8NI16 |
| L | Fab light chain | protein | 214 | 6% helix, 50% strand | — |
| H | Fab heavy chain | protein | 230 | 5% helix, 53% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 380 | 0.56 | 0.74 | 39 | empty |
| 2 | 179 | 0.52 | 0.78 | 23 | empty |
| 3 | 223 | 0.51 | 0.76 | 32 | empty |
| 4 | 51 | 0.50 | 0.88 | 21 | empty |
| 5 | 124 | 0.39 | 0.74 | 25 | empty |
Interfaces
3 interfaces between chains.
- L–H · 2134 Ų buried · 23 hydrogen bonds · protein-protein
- A–H · 1205 Ų buried · 19 hydrogen bonds · protein-protein
- A–L · 345 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 3GRW · FGFR3 in complex with a Fab · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8NI16
- Elsewhere: RCSB PDB 3GRW · PDBe 3GRW · UniProt Q8NI16
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