PDBe 2omh

X-ray diffraction
1.36Å resolution

Structure of human insulin cocrystallized with ARG-12 peptide in presence of urea

Released:
Source organism: Homo sapiens
Primary publication:
Structural characterization of insulin NPH formulations.
Eur J Pharm Sci 30 414-23 (2007)
PMID: 17339105

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
Molecule details ›
Chains: A, C, E
Length: 21 amino acids
Theoretical weight: 2.38 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01308 (Residues: 90-110; Coverage: 24%)
Gene name: INS
Insulin B chain Chains: B, D, F
Molecule details ›
Chains: B, D, F
Length: 30 amino acids
Theoretical weight: 3.43 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01308 (Residues: 25-54; Coverage: 35%)
Gene name: INS

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P43212
Unit cell:
a: 61.36Å b: 61.36Å c: 85.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.2 0.223