› 1ciq

X-ray diffraction
2.2Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dodecamer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133914 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Subtilisin-chymotrypsin inhibitor-2A Chain: A
Molecule details ›
Chain: A
Length: 40 amino acids
Theoretical weight: 4.45 KDa
Source organism: Hordeum vulgare
Expression system: Escherichia coli
UniProt:
  • Canonical: P01053 (Residues: 21-60; Coverage: 48%)
Sequence domains: Potato inhibitor I family
Subtilisin-chymotrypsin inhibitor-2A Chain: B
Molecule details ›
Chain: B
Length: 24 amino acids
Theoretical weight: 2.88 KDa
Source organism: Hordeum vulgare
Expression system: Escherichia coli
UniProt:
  • Canonical: P01053 (Residues: 61-84; Coverage: 29%)
Sequence domains: Potato inhibitor I family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P622
Unit cell:
a: 69.17Å b: 69.17Å c: 53.91Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 not available not available
Expression system: Escherichia coli

Quick links

Citations

6 review citations

From Levinthal to pathways to funnels.
Dill et al. (1997)
5 more

2 mentions without citation

Estimates of protein surface areas in solution by electrospray ionization mass spectrometry.
Kaltashov et al. (2005)
1 more