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Crystal structure of the FGFR2 D2 domain in complex with Fab 2B.1.3

Analyse Crystal structure of the FGFR2 D2 domain in complex with Fab 2B.1.3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4WV1
Type
protein
Length
1,072 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fibroblast growth factor receptor 2; Fab heavy chain; Fab light chain
EC
2.7.10.1
UniProt
P21802
Pockets
11 · best druggability 0.56

Structure

x-ray diffraction · 3 distinct chains · 6% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
F, CFibroblast growth factor receptor 2 (EC 2.7.10.1)protein9812% helix, 51% strandP21802
B, EFab heavy chainprotein2244% helix, 56% strand—
A, DFab light chainprotein2145% helix, 50% strand—

Pockets

11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13450.560.7640empty
23210.560.7636empty
33260.530.7438empty
42170.480.7530empty
51220.470.7933empty

Interfaces

11 interfaces between chains.

  • B–A · 1962 Ų buried · 21 hydrogen bonds · protein-protein
  • E–D · 1954 Ų buried · 21 hydrogen bonds · protein-protein
  • F–E · 826 Ų buried · 15 hydrogen bonds · protein-protein
  • C–B · 812 Ų buried · 15 hydrogen bonds · protein-protein
  • A–D · 293 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

  • 4WV1 · Crystal structure of the FGFR2 D2 domain in complex with Fab 2B.1.3 · the same entry in another collection · chain D against D, TM-score 1.00
  • P21802 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 2 (P21802) · a predicted model of the same protein · chain C against A, TM-score 0.92

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