5KO0: HIAPPWT

Human Islet Amyloid Polypeptide Segment 15-FLVHSSNNFGA-25 Determined by MicroED. Determined by electron crystallography at 1.4 Å resolution. Released 21 Dec 2016.

Method
Electron crystallography
Resolution
1.4 Å
Organism
Homo sapiens
Chains
2
Atoms
179
Mol. weight
2.44 kDa
Ligands
SCN
Released
21 Dec 2016

Explore 5KO0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5KO0 contains 0 α-helices and 2 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A and B: 0 helices, 1 β-strand

ElementResiduesLengthSheet
β-strand16-2491

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
hIAPP(15-25)WTA, Bprotein11Homo sapiensP10997 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5KO0_1 hIAPP(15-25)WT (chains A, B)
FLVHSSNNFGA

Ligands and cofactors

IDNameFormulaCopies
SCNThiocyanate ionC N S1

Primary citation

Atomic structures of fibrillar segments of hIAPP suggest tightly mated beta-sheets are important for cytotoxicity. Krotee, P., Rodriguez, J.A., Sawaya, M.R. et al. Elife (2017) 6. DOI 10.7554/eLife.19273 · PubMed

Other PDB entries of the same protein (UniProt P10997 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

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