Research workbench
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag and leu 44 replaced by phe (L44F)
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
- 1JTC
- Type
- protein
- Length
- 564 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acidic fibroblast growth factor
- UniProt
- P05230
- Pockets
- 4 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Acidic fibroblast growth factor | protein | 141 | 6% helix, 38% strand | P05230 |
Ligands and binding sites
- FMT · Formic acid · additive · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.41 | 0.77 | 19 | empty |
| 2 | 106 | 0.41 | 0.77 | 21 | empty |
| 3 | 51 | 0.40 | 0.82 | 13 | empty |
| 4 | 56 | 0.39 | 0.81 | 16 | empty |
Interfaces
2 interfaces between chains.
- C–D · 441 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 441 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1JTC · Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag… · 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
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 1JTC · PDBe 1JTC · UniProt P05230
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