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Crystal structure of L44F/C83T/C117V/F132W mutant of human acidic fibroblast growth factor

Analyse Crystal structure of L44F/C83T/C117V/F132W mutant of human acidic fibroblast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3FGM
Type
protein
Length
282 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heparin-binding growth factor 1
UniProt
Q5NVQ3
Ligands
SO4
Pockets
3 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHeparin-binding growth factor 1protein1416% helix, 38% strandQ5NVQ3

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A, B
  • FMT · Formic acid · additive · 3 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11260.410.7624empty
2580.370.7917empty
3600.310.7524empty

Interfaces

1 interface between chains.

  • A–B · 418 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 3FGM · Crystal structure of L44F/C83T/C117V/F132W mutant of Human acidic fibroblast growth factor · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5NVQ3 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 1 (Q5NVQ3) · a predicted model of the same protein · chain A against A, TM-score 0.97

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