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Crystal structure of A66C mutant of human acidic fibroblast growth factor

Analyse Crystal structure of A66C mutant of human acidic fibroblast growth factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3FJK
Type
protein
Length
565 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heparin-binding growth factor 1
UniProt
P05230
Ligands
SO4
Pockets
3 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHeparin-binding growth factor 1protein1426% helix, 37% strandP05230
B, C, DHeparin-binding growth factor 1protein14111% helix, 38% strandP05230

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains B, C
  • FMT · Formic acid · additive · 2 copies · chains B, D

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16490.750.8166empty
21980.690.8732empty
33760.650.7943empty

Interfaces

5 interfaces between chains.

  • A–B · 633 Ų buried · 17 hydrogen bonds · protein-protein
  • C–D · 611 Ų buried · 19 hydrogen bonds · protein-protein
  • A–C · 516 Ų buried · 0 hydrogen bonds · protein-protein
  • B–D · 513 Ų buried · 0 hydrogen bonds · protein-protein
  • A–D · 147 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 3FJK · Crystal structure of A66C mutant of Human acidic fibroblast growth factor · 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 B against A, TM-score 0.96

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