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Crystal structure of human FGF18

Analyse Crystal structure of human FGF18 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4CJM
Type
protein
Length
514 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fibroblast growth factor 18
UniProt
O76093
Ligands
SO4
Pockets
2 · best druggability 0.46

Structure

x-ray diffraction · 3 distinct chains · 9% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFibroblast growth factor 18protein1299% helix, 41% strandO76093
B, CFibroblast growth factor 18protein1289% helix, 41% strandO76093
DFibroblast growth factor 18protein1299% helix, 43% strandO76093

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 13 copies · chains A, D, B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11920.460.7525empty
2610.330.7713empty

Interfaces

3 interfaces between chains.

  • A–B · 492 Ų buried · 8 hydrogen bonds · protein-protein
  • A–D · 476 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 321 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 4CJM · Crystal structure of human FGF18 · the same entry in another collection · chain D against D, TM-score 1.00
  • O76093 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 18 (O76093) · a predicted model of the same protein · chain D against A, TM-score 0.98

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