Compound record
Insulin (human)
Human insulin; insulin human; rDNA insulin
Sequence
A-chain GIVEQCCTSICSLYQLENYCN; B-chain FVNQHLCGSHLVEALYLVCGERGFFYTPKT; disulfides A6–A11, A7–B7, A20–B19
GIVEQCCTSICSLYQLENYCN FVNQHLCGSHLVEALYLVCGERGFFYTPKT
Length counts residues; formula and mass are the stored free-base values from cited sources; CAS and PubChem identify the substance in public registries. More detail: length & peptide bonds, molecular weight
Structure & modifications
Classified cyclic because of intramolecular (including interchain) disulfides. Sequence field lists A then B.
Notes
Mature human insulin is a two-chain hormone: A21 + B30 (51 residues total), covalently joined by disulfides rather than expressed as one continuous polymer.
Disulfide map
| Bridge | Type | Residues |
|---|---|---|
| Intra-A | Intrachain | A6–A11 |
| Interchain 1 | A–B | A7–B7 |
| Interchain 2 | A–B | A20–B19 |
Because those links create covalent rings, this database classifies insulin as cyclic even though each chain is written linearly. The sequence field lists A then B (space-separated).
Proinsulin, insulin lispro, aspart, glargine, and other analogues are different chemical entities. This CAS/PubChem pair is free-base human insulin only (11061-68-0 / 118984375).
Zinc hexamers and pharmaceutical salts are formulation states of the same covalent backbone, not alternate sequences.
Primary-source references
- PubChem CID 118984375 — insulin human
- UniProt P01308 (insulin, Homo sapiens)
- Ryle A.P. et al. The disulphide bonds of insulin. Biochem. J. 1955.