Research workbench
Human fibroblast growth factor - 1 (FGF-1) mutant S116R
Analyse Human fibroblast growth factor - 1 (FGF-1) mutant S116R in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XKI
- Type
- protein
- Length
- 289 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibroblast growth factor 1
- UniProt
- P05230
- Ligands
- PO4, SO4
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibroblast growth factor 1 | protein | 145 | 8% helix, 37% strand | P05230 |
| B | Fibroblast growth factor 1 | protein | 144 | 8% helix, 38% strand | P05230 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 8 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · chains A, B
- 2PE · Nonaethylene glycol · additive · 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 | 220 | 0.63 | 0.82 | 40 | empty |
| 2 | 197 | 0.56 | 0.79 | 28 | empty |
| 3 | 133 | 0.54 | 0.81 | 30 | 2PE |
Interfaces
1 interface between chains.
- A–B · 531 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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
- Elsewhere: RCSB PDB 4XKI · PDBe 4XKI · UniProt P05230
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