PDBe 1htv

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of destripeptide (B28-B30) insulin: implications for insulin dissociation.
Biochim. Biophys. Acta 1547 18-25 (2001)
PMID: 11343787

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
hetero 12-mer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Insulin A chain Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 21 amino acids
Theoretical weight: 2.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01308 (Residues: 90-110; Coverage: 24%)
Gene name: INS
Insulin B chain Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 27 amino acids
Theoretical weight: 3.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01308 (Residues: 25-51; Coverage: 31%)
Gene name: INS

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 49.81Å b: 51.55Å c: 100.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.196 0.24
Expression system: Escherichia coli