› 1w8p

X-ray diffraction
2.08Å resolution

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

Released:
DOI: 10.2210/pdb1w8p/pdb
PDB entry 1w8p coloured by chain, front view.
PDB entry 1w8p coloured by chain, side view.
PDB entry 1w8p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Toward the insulin-IGF-I intermediate structures: functional and structural properties of the [TyrB25NMePheB26] insulin mutant.
Záková L, Brynda J, Au-Alvarez O, Dodson EJ, Dodson GG, Whittingham JL, Brzozowski AM
Biochemistry 43 16293-300 (2004)
PMID: 15610023

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134235 (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
Sequence domains: Insulin/IGF/Relaxin family

Ligands and Environments

2 bound ligands:
Ligand IPH 6 x IPH
Ligand ZN 2 x ZN
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

Quick links

Citations

6 citation in other articles

Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues.
Jirácek et al. (2010)
5 more

1 mention without citation

Non-equivalent role of inter- and intramolecular hydrogen bonds in the insulin dimer interface.
Antolíková et al. (2011)