Research workbench
Crystal structure of FGF1 complexed with the ectodomain of FGFR2B harboring the A172F pfeiffer syndrome mutation
Analyse Crystal structure of FGF1 complexed with the ectodomain of FGFR2B harboring the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OJ2
- Type
- protein
- Length
- 688 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heparin-binding growth factor 1; Fibroblast growth factor receptor 2
- EC
- 2.7.10.1
- UniProt
- P05230, P21802
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Heparin-binding growth factor 1 | protein | 135 | 9% helix, 39% strand | P05230 |
| C, D | Fibroblast growth factor receptor 2 (EC 2.7.10.1) | protein | 209 | 5% helix, 51% strand | P21802 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B, C
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 | 953 | 0.73 | 0.77 | 119 | empty |
| 2 | 473 | 0.62 | 0.75 | 57 | empty |
| 3 | 140 | 0.53 | 0.81 | 20 | empty |
| 4 | 158 | 0.52 | 0.79 | 21 | empty |
| 5 | 76 | 0.33 | 0.75 | 22 | empty |
Interfaces
5 interfaces between chains.
- A–C · 1492 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 1470 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 971 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 119 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 99 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3OJ2 · Crystal structure of FGF1 complexed with the ectodomain of FGFR2b harboring the A172F… · the same entry in another collection · chain D against D, 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 0.96
- P21802 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 2 (P21802) · a predicted model of the same protein · chain D against A, TM-score 0.61
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 P21802
- Elsewhere: RCSB PDB 3OJ2 · PDBe 3OJ2 · UniProt P05230 · UniProt P21802
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.