PDBe 1w8p

X-ray diffraction
2.08Å resolution

Structural properties of the B25Tyr-NMe-B26Phe insulin mutant.

Released:

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: Saccharomyces cerevisiae
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: 30 amino acids
Theoretical weight: 3.43 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P01308 (Residues: 25-54; Coverage: 35%)
Gene name: INS

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P21
Unit cell:
a: 59.903Å b: 62.116Å c: 47.796Å
α: 90° β: 110.58° γ: 90°
R-values:
R R work R free
0.192 0.189 0.256
Expression system: Saccharomyces cerevisiae