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Crystal structure of SER252TRP apert mutant FGF receptor 2 (FGFR2) in complex with FGF2

Analyse Crystal structure of SER252TRP apert mutant FGF receptor 2 (FGFR2) in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1II4
Type
protein
Length
1,336 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heparin-binding growth factor 2; Fibroblast growth factor receptor 2
EC
2.7.1.112
UniProt
P09038, P21802
Pockets
11 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DHeparin-binding growth factor 2protein1344% helix, 41% strandP09038
E, F, G, HFibroblast growth factor receptor 2 (EC 2.7.1.112)protein2009% helix, 51% strandP21802

Pockets

11 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110720.770.79125empty
26960.690.7787empty
31860.600.8233empty
41710.600.8333empty
51530.590.8423empty

Interfaces

13 interfaces between chains.

  • A–E · 1603 Ų buried · 20 hydrogen bonds · protein-protein
  • D–H · 1596 Ų buried · 22 hydrogen bonds · protein-protein
  • C–G · 1594 Ų buried · 22 hydrogen bonds · protein-protein
  • B–F · 1590 Ų buried · 18 hydrogen bonds · protein-protein
  • F–G · 989 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

  • 1II4 · Crystal structure of SER252TRP apert mutant FGF receptor 2 (FGFR2) in complex with FGF2 · the same entry in another collection · chain H against H, TM-score 1.00
  • P09038 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 2 (P09038) · a predicted model of the same protein · chain C against A, TM-score 0.96

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