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MolNFT v1 · #16296 · protein

Crystal structure analysis of the FGF10-FGFR2B complex

1NUN · Fibroblast growth factor-10: “Crystal structure analysis of the FGF10-FGFR2B complex”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.53). MolNFT v1 #16296 on GenesisL1: 3D structure, binding sites and pockets in…

PDB
1NUN
Type
protein
Length
348 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fibroblast growth factor-10; Fibroblast growth factor receptor 2 isoform 2
UniProt
O15520, P21802
Ligands
SO4
Pockets
2 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFibroblast growth factor-10protein1397% helix, 48% strandO15520
BFibroblast growth factor receptor 2 isoform 2protein2096% helix, 49% strandP21802

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains A
  • 15P · Polyethylene glycol (N=34) · additive · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11850.530.7833empty
21830.490.7624empty

Interfaces

1 interface between chains.

  • A–B · 1454 Ų buried · 25 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified, 1 disulfide (engineered, disulfide).

Compared structures

  • 1NUN · Crystal Structure Analysis of the FGF10-FGFR2b Complex · the same entry in another collection · chain A against A, TM-score 1.00
  • O15520 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 10 (O15520) · a predicted model of the same protein · chain A against A, TM-score 0.97
  • P21802 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 2 (P21802) · a predicted model of the same protein · chain B against A, TM-score 0.63

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