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An ultra-stable single-chain insulin analog resists thermal inactivation and exhibits biological signaling duration equivalent to the native protein

Analyse An ultra-stable single-chain insulin analog resists thermal inactivation and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5WDM
Type
protein
Length
273 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Single-chain insulin analog
UniProt
A6XGL2
Pockets
5 · best druggability 0.60

Structure

x-ray diffraction · 4 distinct chains · 49% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASingle-chain insulin analogprotein4549% helix, 9% strandA6XGL2
BSingle-chain insulin analogprotein4650% helix, 9% strandA6XGL2
C, FSingle-chain insulin analogprotein4448% helix, 9% strandA6XGL2
D, ESingle-chain insulin analogprotein4749% helix, 9% strandA6XGL2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12680.600.7930empty
2820.510.8321empty
31640.490.7723empty
41480.450.7626empty
5890.430.7812empty

Interfaces

13 interfaces between chains.

  • E–F · 588 Ų buried · 9 hydrogen bonds · protein-protein
  • C–D · 514 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 502 Ų buried · 5 hydrogen bonds · protein-protein
  • A–F · 493 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 387 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

  • 5WDM · An ultra-stable single-chain insulin analog resists thermal inactivation and exhibits… · the same entry in another collection · chain A against A, TM-score 1.00

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