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Modified A22GLY-B31ARG human insulin

Analyse Modified A22GLY-B31ARG human insulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2LGB
Type
protein
Length
53 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Insulin a chain; Insulin B chain
UniProt
P01308

Structure

solution nmr · 2 distinct chains · 45% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInsulin a chainprotein2259% helix, 5% strandP01308
BInsulin B chainprotein3135% helix, 3% strandP01308

Interfaces

1 interface between chains.

  • A–B · 814 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 2LGB · Modified A22Gly-B31Arg Human Insulin · the same entry in another collection · chain A against A, TM-score 1.00

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