Research workbench
Fgfr tyrosine kinase domain in complex with 3-(3-methoxybenzyl)-7- azaindole
Analyse Fgfr tyrosine kinase domain in complex with 3-(3-methoxybenzyl)-7- azaindole in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C4F
- Type
- protein
- Length
- 580 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Basic fibroblast growth factor receptor 1
- EC
- 2.7.10.1
- UniProt
- P11362
- Ligands
- C4F
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Basic fibroblast growth factor receptor 1 (EC 2.7.10.1) | protein | 290 | 41% helix, 13% strand | P11362 |
Ligands and binding sites
- C4F · 3-(3-methoxybenzyl)-1H-pyrrolo[2,3-b]pyridine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.75 | 0.78 | 100 | empty |
| 2 | 714 | 0.75 | 0.80 | 65 | C4F |
| 3 | 666 | 0.74 | 0.80 | 69 | C4F |
Interfaces
1 interface between chains.
- A–B · 502 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3C4F · FGFR TYROSINE KINASE DOMAIN IN COMPLEX WITH 3-(3-methoxybenzyl)-7-azaindole · the same entry in another collection · chain A against A, TM-score 1.00
- P11362 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 1 (P11362) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P11362
- Elsewhere: RCSB PDB 3C4F · PDBe 3C4F · UniProt P11362
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