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The insulin receptor ectodomain in complex with three venom hybrid insulin molecules - asymmetric conformation

Analyse The insulin receptor ectodomain in complex with three venom hybrid insulin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7MQS
Type
protein
Length
1,739 residues
Chains
8
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Isoform short of insulin receptor; Insulin a chain; Insulin B chain
EC
2.7.10.1
UniProt
P01308
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 5 distinct chains · 9% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
EIsoform short of insulin receptor (EC 2.7.10.1)protein8068% helix, 31% strand—
FIsoform short of insulin receptor (EC 2.7.10.1)protein8118% helix, 29% strand—
A, C, GInsulin a chainprotein2446% helix, 0% strandP01308
B, DInsulin B chainprotein1656% helix, 0% strandP01308
HInsulin B chainprotein1850% helix, 0% strandP01308

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12950.850.9451empty
27900.810.8473empty
38700.790.8285empty
4770.730.9625empty
51300.710.9131empty

Interfaces

14 interfaces between chains.

  • E–F · 2722 Ų buried · 29 hydrogen bonds · protein-protein
  • F–A · 677 Ų buried · 9 hydrogen bonds · protein-protein
  • G–H · 542 Ų buried · 1 hydrogen bond · protein-protein
  • C–D · 475 Ų buried · 2 hydrogen bonds · protein-protein
  • E–G · 441 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 44 disulfide (disulfide).

Compared structures

  • 7MQS · The insulin receptor ectodomain in complex with three venom hybrid insulin molecules… · the same entry in another collection · chain E against E, TM-score 1.00

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