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Crystal structure of C117S mutant of human acidic fibroblast growth factor

Analyse Crystal structure of C117S 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
4QC4
Type
protein
Length
282 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fibroblast growth factor 1
UniProt
P05230
Ligands
NA
Pockets
1 · best druggability 0.39

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BFibroblast growth factor 1protein1416% helix, 38% strandP05230

Ligands and binding sites

  • NA · Sodium ion · metal · chains A
  • FLC · Citrate anion · additive · 2 copies · chains A, B
  • IMD · Imidazole · additive · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1970.390.7619IMD

Interfaces

1 interface between chains.

  • A–B · 460 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 4QC4 · Crystal structure of C117S mutant of human acidic fibroblast growth factor · 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

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