Research workbench
X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. a completely inactive analogue
Analyse X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6INS
- Type
- protein
- Length
- 100 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin
- UniProt
- P01315
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, F | Insulin | protein | 50 | 62% helix, 8% strand | P01315 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- E–F · 647 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 6INS · X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. a completely… · the same entry in another collection · chain E against E, 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 P01315
- Elsewhere: RCSB PDB 6INS · PDBe 6INS · UniProt P01315
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