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Full-length insulin receptor bound with site 2 binding deficient mutant insulin (B-L17R) -- symmetric conformation

Analyse Full-length insulin receptor bound with site 2 binding deficient mutant insulin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7SL6
Type
protein
Length
1,734 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Insulin receptor; Insulin B chain; Insulin a chain
EC
2.7.10.1
UniProt
P15208, P01308
Pockets
20 · best druggability 0.76

Structure

electron microscopy · 3 distinct chains · 15% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BInsulin receptor (EC 2.7.10.1)protein81913% helix, 30% strandP15208
E, FInsulin B chainprotein2737% helix, 4% strandP01308
C, DInsulin a chainprotein2157% helix, 5% strandP01308

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19800.760.7971empty
29270.760.7981empty
34500.690.8054empty
43020.620.7938empty
53820.620.7741empty

Interfaces

11 interfaces between chains.

  • A–B · 2798 Ų buried · 24 hydrogen bonds · protein-protein
  • E–C · 670 Ų buried · 11 hydrogen bonds · protein-protein
  • F–D · 664 Ų buried · 11 hydrogen bonds · protein-protein
  • A–F · 524 Ų buried · 1 hydrogen bond · protein-protein
  • B–E · 523 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 40 disulfide (disulfide).

Compared structures

  • 7SL6 · Full-length insulin receptor bound with site 2 binding deficient mutant insulin (B-L17R)… · the same entry in another collection · chain E against E, TM-score 1.00
  • P15208 · AlphaFold monomer V2.0 prediction for insulin receptor (P15208) · a predicted model of the same protein · chain A against A, TM-score 0.49

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