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Cryo-EM structure of human insulin degrading enzyme

Analyse Cryo-EM structure of human insulin degrading enzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6B7Y
Type
protein
Length
1,888 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Insulin-degrading enzyme
EC
3.4.24.56
UniProt
P14735
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 2 distinct chains · 43% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInsulin-degrading enzyme (EC 3.4.24.56)protein94942% helix, 16% strandP14735
BInsulin-degrading enzyme (EC 3.4.24.56)protein93943% helix, 16% strandP14735

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111740.860.87102empty
21980.820.9545empty
32170.810.9350empty
41690.800.9542empty
51070.790.9833empty

Interfaces

1 interface between chains.

  • A–B · 1390 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 6B7Y · Cryo-EM structure of human insulin degrading enzyme · the same entry in another collection · chain A against A, TM-score 1.00

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