Research workbench
Human fibroblast growth factor-1 C16S/A66C/C117A/P134A
Analyse Human fibroblast growth factor-1 C16S/A66C/C117A/P134A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YOL
- Type
- protein
- Length
- 286 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.97
- Source
- Homo sapiens
- Molecule
- Fibroblast growth factor 1
- UniProt
- P05230
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · resolution 1.97 · 1 distinct chain · 6% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fibroblast growth factor 1 | protein | 143 | 6% helix, 37% strand | P05230 |
Ligands and binding sites
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 | 214 | 0.60 | 0.81 | 36 | empty |
| 2 | 197 | 0.57 | 0.80 | 33 | empty |
| 3 | 130 | 0.50 | 0.80 | 27 | IMD |
Interfaces
1 interface between chains.
- A–B · 491 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 4YOL · PDBe 4YOL · UniProt P05230
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