Research workbench
Human Insulin
Analyse Human Insulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EWW
- Type
- protein
- Length
- 102 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Homo sapiens
- Molecule
- Insulin A chain; Insulin B chain
- UniProt
- P01308
- Ligands
- ZN, CL
Structure
x-ray diffraction · resolution 2.3 · 2 distinct chains · 55% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Insulin A chain | protein | 21 | 67% helix, 14% strand | P01308 |
| B, D | Insulin B chain | protein | 30 | 47% helix, 17% strand | P01308 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- C–D · 909 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 902 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 608 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 53 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 44 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 4EWW · Human insulin · 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 4EWW · PDBe 4EWW · UniProt P01308
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