Research workbench
Human islet amyloid polypeptide segment 15-flvhssnnfga-25 determined by microed
Analyse Human islet amyloid polypeptide segment 15-flvhssnnfga-25 determined by microed in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KO0
- Type
- protein
- Length
- 22 residues
- Chains
- 2
- Method
- electron crystallography
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIAPP(15-25)WT
- UniProt
- P10997
- Ligands
- SCN
Structure
electron crystallography · 1 distinct chain · 0% helix, 82% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | HIAPP(15-25)WT | protein | 11 | 0% helix, 82% strand | P10997 |
Ligands and binding sites
- SCN · Thiocyanate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 489 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 5KO0 · Human Islet Amyloid Polypeptide Segment 15-FLVHSSNNFGA-25 Determined by MicroED · 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 0.26
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 5KO0 · PDBe 5KO0 · UniProt P10997
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