Research workbench
Crystal structure of the 3 ig form of FGFR3C in complex with FGF1
Analyse Crystal structure of the 3 ig form of FGFR3C in complex with FGF1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RY7
- Type
- protein
- Length
- 364 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heparin-binding growth factor 1; Fibroblast growth factor receptor 3
- UniProt
- P05230, P22607
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heparin-binding growth factor 1 | protein | 151 | 10% helix, 24% strand | P05230 |
| B | Fibroblast growth factor receptor 3 | protein | 213 | 3% helix, 36% strand | P22607 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.54 | 0.78 | 27 | empty |
| 2 | 226 | 0.50 | 0.75 | 26 | empty |
| 3 | 152 | 0.42 | 0.74 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 1547 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 1RY7 · Crystal Structure of the 3 Ig form of FGFR3c in complex with FGF1 · the same entry in another collection · chain A against A, TM-score 1.00
- P05230 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 1 (P05230) · a predicted model of the same protein · chain A against A, TM-score 0.86
- P22607 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 3 (P22607) · a predicted model of the same protein · chain B against A, TM-score 0.60
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 P05230
- Every structure of UniProt P22607
- Elsewhere: RCSB PDB 1RY7 · PDBe 1RY7 · UniProt P05230 · UniProt P22607
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