Research workbench
Ligand controlled assembly of hexamers, dihexamers, and linear multihexamer structures by an engineered acylated insulin
Analyse Ligand controlled assembly of hexamers, dihexamers, and linear multihexamer… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AK0
- Type
- protein
- Length
- 50 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.28
- Source
- HOMO SAPIENS
- Molecule
- Insulin a chain; Insulin B chain
- UniProt
- P01308
Structure
x-ray diffraction · resolution 2.28 · 2 distinct chains · 50% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin a chain | protein | 21 | 52% helix, 5% strand | P01308 |
| B | Insulin B chain | protein | 29 | 48% helix, 3% strand | P01308 |
Interfaces
1 interface between chains.
- A–B · 763 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 4AK0 · Ligand controlled assembly of hexamers, dihexamers, and linear multihexamer structures by… · the same entry in another collection · chain A against A, TM-score 1.00
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 P01308
- Elsewhere: RCSB PDB 4AK0 · PDBe 4AK0 · UniProt P01308
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