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Crystal structure of FGFR4 domain 3 in complex with a de novo-designed mini-binder

Analyse Crystal structure of FGFR4 domain 3 in complex with a de novo-designed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7N1J
Type
protein
Length
355 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fibroblast growth factor receptor 4; Binder
EC
2.7.10.1
UniProt
P22455
Pockets
1 · best druggability 0.62

Structure

x-ray diffraction · 4 distinct chains · 32% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFibroblast growth factor receptor 4 (EC 2.7.10.1)protein1252% helix, 44% strandP22455
BBinderprotein6481% helix, 0% strand—
CFibroblast growth factor receptor 4 (EC 2.7.10.1)protein1033% helix, 52% strandP22455
DBinderprotein6386% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11180.620.8733empty

Interfaces

6 interfaces between chains.

  • A–B · 864 Ų buried · 8 hydrogen bonds · protein-protein
  • C–D · 852 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 390 Ų buried · 5 hydrogen bonds · protein-protein
  • B–D · 201 Ų buried · 6 hydrogen bonds · protein-protein
  • A–D · 189 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 7N1J · Crystal structure of FGFR4 domain 3 in complex with a de novo-designed mini-binder · the same entry in another collection · chain A against A, TM-score 1.00
  • P22455 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 4 (P22455) · a predicted model of the same protein · chain C against A, TM-score 0.92

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