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Complex structure of E4 mutant human IGF2R domain 11 bound to igf-II

Analyse Complex structure of E4 mutant human IGF2R domain 11 bound to igf-II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2L29
Type
protein
Length
209 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Insulin-like growth factor 2 receptor variant; Insulin-like growth factor II
UniProt
Q59EZ3, P01344
Pockets
2 · best druggability 0.58

Structure

solution nmr · 2 distinct chains · 12% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInsulin-like growth factor 2 receptor variantprotein1422% helix, 44% strandQ59EZ3
BInsulin-like growth factor IIprotein6733% helix, 1% strandP01344

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1860.580.8725empty
2810.350.7616empty

Interfaces

1 interface between chains.

  • A–B · 775 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

  • 2L29 · Complex structure of E4 mutant human IGF2R domain 11 bound to IGF-II · the same entry in another collection · chain B against B, TM-score 1.00
  • P01344 · AlphaFold monomer V2.0 prediction for insulin-like growth factor II (P01344) · a predicted model of the same protein · chain B against A, TM-score 0.58

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