GL1X · GenesisL1 explorer

Research workbench

Solution NMR structure of human amylin in sds micelles at pH 7.3

Analyse Solution NMR structure of human amylin in sds micelles at pH 7.3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2L86
Type
protein
Length
37 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Islet amyloid polypeptide
UniProt
P10997
Ligands
NH2

Structure

solution nmr · 1 distinct chain · 51% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIslet amyloid polypeptideprotein3751% helix, 0% strandP10997

Ligands and binding sites

  • NH2 · Amino group · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 2L86 · Solution NMR structure of human amylin in SDS micelles at pH 7.3 · the same entry in another collection · chain A against A, TM-score 1.00
  • P10997 · AlphaFold monomer V2.0 prediction for islet amyloid polypeptide (P10997) · a predicted model of the same protein · chain A against A, TM-score 0.39

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.