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Human insulin mutant A22GLY-B31LYS-B32ARG

Analyse Human insulin mutant A22GLY-B31LYS-B32ARG in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2KXK
Type
protein
Length
54 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Insulin a chain; Insulin B chain
UniProt
P01308
Pockets
1 · best druggability 0.31

Structure

solution nmr · 2 distinct chains · 35% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInsulin a chainprotein2236% helix, 5% strandP01308
BInsulin B chainprotein3234% helix, 3% strandP01308

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.310.7610empty

Interfaces

1 interface between chains.

  • A–B · 924 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 2KXK · Human Insulin Mutant A22Gly-B31Lys-B32Arg · the same entry in another collection · chain A against A, TM-score 1.00

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