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Low resolution cryo-EM structure of the full-length insulin receptor bound to 2 insulin, conf 3

Analyse Low resolution cryo-EM structure of the full-length insulin receptor bound to 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7PG4
Type
protein
Length
1,698 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Isoform short of insulin receptor; Insulin
EC
2.7.10.1
UniProt
P06213, P01308
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 5 distinct chains · 11% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIsoform short of insulin receptor (EC 2.7.10.1)protein7868% helix, 32% strandP06213
BIsoform short of insulin receptor (EC 2.7.10.1)protein82212% helix, 27% strandP06213
C, IInsulinprotein2157% helix, 0% strandP01308
DInsulinprotein2536% helix, 0% strandP01308
JInsulinprotein2343% helix, 4% strandP01308

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14670.850.9156empty
22860.840.9454empty
31890.820.9542empty
4970.760.9635empty
58840.680.7466empty

Interfaces

9 interfaces between chains.

  • A–B · 2589 Ų buried · 17 hydrogen bonds · protein-protein
  • C–D · 604 Ų buried · 7 hydrogen bonds · protein-protein
  • I–J · 593 Ų buried · 8 hydrogen bonds · protein-protein
  • B–D · 549 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 436 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 44 disulfide (disulfide).

Compared structures

  • 7PG4 · Low resolution Cryo-EM structure of the full-length insulin receptor bound to 2 insulin… · the same entry in another collection · chain A against A, TM-score 1.00

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