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Solution structure of oxidized and amidated human iapp (1-37), the diabetes II peptide.
Analyse Solution structure of oxidized and amidated human iapp (1-37), the diabetes II… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MGQ
- Type
- protein
- Length
- 37 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Islet amyloid polypeptide
- UniProt
- P10997
Structure
solution nmr · 1 distinct chain · 22% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Islet amyloid polypeptide | protein | 37 | 22% helix, 0% strand | P10997 |
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, nonstandard).
Compared structures
- 5MGQ · Solution structure of oxidized and amidated human IAPP (1-37), the diabetes II peptide. · 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 0.32
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P10997
- Elsewhere: RCSB PDB 5MGQ · PDBe 5MGQ · UniProt P10997
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