Research workbench
Crystal structure of PRO253ARG apert mutant FGF receptor 2 (FGFR2) in complex with FGF2
Analyse Crystal structure of PRO253ARG apert mutant FGF receptor 2 (FGFR2) in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IIL
- Type
- protein
- Length
- 1,361 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heparin-binding growth factor 2; Fibroblast growth factor receptor 2
- EC
- 2.7.1.112
- UniProt
- P09038, P21802
- Pockets
- 16 · best druggability 0.70
Structure
x-ray diffraction · 6 distinct chains · 8% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heparin-binding growth factor 2 | protein | 134 | 7% helix, 41% strand | P09038 |
| B | Heparin-binding growth factor 2 | protein | 133 | 7% helix, 41% strand | P09038 |
| C | Heparin-binding growth factor 2 | protein | 132 | 9% helix, 42% strand | P09038 |
| D | Heparin-binding growth factor 2 | protein | 132 | 9% helix, 42% strand | P09038 |
| E, F | Fibroblast growth factor receptor 2 (EC 2.7.1.112) | protein | 200 | 10% helix, 51% strand | P21802 |
| G, H | Fibroblast growth factor receptor 2 (EC 2.7.1.112) | protein | 215 | 9% helix, 47% strand | P21802 |
Pockets
16 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 666 | 0.70 | 0.78 | 60 | empty |
| 2 | 532 | 0.65 | 0.76 | 60 | empty |
| 3 | 416 | 0.63 | 0.77 | 50 | empty |
| 4 | 490 | 0.63 | 0.76 | 57 | empty |
| 5 | 277 | 0.63 | 0.80 | 41 | empty |
Interfaces
14 interfaces between chains.
- B–F · 1598 Ų buried · 21 hydrogen bonds · protein-protein
- A–E · 1583 Ų buried · 22 hydrogen bonds · protein-protein
- D–H · 1534 Ų buried · 22 hydrogen bonds · protein-protein
- C–G · 1482 Ų buried · 22 hydrogen bonds · protein-protein
- E–H · 1119 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1IIL · Crystal structure of PRO253ARG apert mutant FGF receptor 2 (FGFR2) in complex with FGF2 · the same entry in another collection · chain H against H, TM-score 1.00
- P09038 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 2 (P09038) · a predicted model of the same protein · chain C 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 P09038
- Every structure of UniProt P21802
- Elsewhere: RCSB PDB 1IIL · PDBe 1IIL · UniProt P09038 · UniProt P21802
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