› 2g4m

X-ray diffraction
1.8Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-134237 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Insulin A chain Chain: A
Molecule details ›
Chain: A
Length: 21 amino acids
Theoretical weight: 2.38 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P01315 (Residues: 88-108; Coverage: 25%)
Gene name: INS
Insulin B chain Chain: B
Molecule details ›
Chain: B
Length: 30 amino acids
Theoretical weight: 3.4 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P01315 (Residues: 25-54; Coverage: 36%)
Gene name: INS
Sequence domains: Insulin/IGF/Relaxin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: I213
Unit cell:
a: 78.27Å b: 78.27Å c: 78.27Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.167 0.223

Quick links

Citations

5 review citations

Conformational selection in trypsin-like proteases.
Pozzi et al. (2012)
4 more

6 mentions without citation

Progress in Simulation Studies of Insulin Structure and Function.
Gorai et al. (2022)
5 more