Research workbench
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag and leu 73 replaced by val and val 109 replaced by leu (L73V/V109L)
Analyse Human acidic fibroblast growth factor. 141 amino acid form with amino terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JT5
- Type
- protein
- Length
- 284 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acidic fibroblast growth factor
- UniProt
- P05230
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acidic fibroblast growth factor | protein | 142 | 6% helix, 37% strand | P05230 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 156 | 0.43 | 0.75 | 19 | empty |
| 2 | 55 | 0.40 | 0.81 | 18 | empty |
| 3 | 58 | 0.25 | 0.72 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 437 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1JT5 · Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag… · the same entry in another collection · chain A against A, 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
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 1JT5 · PDBe 1JT5 · UniProt P05230
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