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Acidic Fibroblast Growth Factor (FGF-1) complexed with gentisic acid

Analyse Acidic Fibroblast Growth Factor (FGF-1) complexed with gentisic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3JUT
Type
protein
Length
780 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.25
Source
Homo sapiens
Molecule
Heparin-binding growth factor 1
UniProt
P05230
Ligands
GTQ
Pockets
4 · best druggability 0.64

Structure

x-ray diffraction · resolution 2.25 · 1 distinct chain · 12% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FHeparin-binding growth factor 1protein13012% helix, 42% strandP05230

Ligands and binding sites

  • GTQ · 2,5-dihydroxybenzoic acid · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14880.640.7652empty
21310.500.8022empty
31770.470.7528empty
4560.310.7617empty

Interfaces

6 interfaces between chains.

  • D–E · 605 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 499 Ų buried · 7 hydrogen bonds · protein-protein
  • D–F · 455 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 239 Ų buried · 1 hydrogen bond · protein-protein
  • E–F · 127 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 3JUT · Acidic fibroblast growth factor (FGF-1) complexed with gentisic acid · the same entry in another collection · chain F against F, TM-score 1.00
  • P05230 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 1 (P05230) · a predicted model of the same protein · chain D against A, TM-score 0.99

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