› 6ins

X-ray diffraction
2Å resolution

X-RAY ANALYSIS OF THE SINGLE CHAIN B29-A1 PEPTIDE-LINKED INSULIN MOLECULE. A COMPLETELY INACTIVE ANALOGUE

Released:
DOI: 10.2210/pdb6ins/pdb
PDB entry 6ins coloured by chain, front view.
PDB entry 6ins coloured by chain, side view.
PDB entry 6ins coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue.
Derewenda U, Derewenda Z, Dodson EJ, Dodson GG, Bing X, Markussen J
J Mol Biol 220 425-33 (1991)
PMID: 1856866

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-134241 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Insulin B chain Chains: E, F
Molecule details ›
Chains: E, F
Length: 50 amino acids
Theoretical weight: 5.7 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P01315 (Residues: 25-108; Coverage: 60%)
Gene name: INS
Sequence domains: Insulin/IGF/Relaxin family
Structure domains: Insulin-like

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R3
Unit cell:
a: 79.22Å b: 79.22Å c: 37.75Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 not available not available
Expression system: Not provided

Quick links

Citations

19 review citations

The role of assembly in insulin's biosynthesis.
Dodson et al. (1998)
18 more

20 mentions without citation

Structural diversity and biological significance of glycosphingolipids in pathogenic and opportunistic fungi.
Guimarães et al. (2014)
19 more