1hja

X-ray diffraction
2.3Å resolution

LYS 18 VARIANT OF TURKEY OVOMUCOID INHIBITOR THIRD DOMAIN COMPLEXED WITH ALPHA-CHYMOTRYPSIN

Released:
Source organisms:
Entry authors: Ding J-H, James MNG

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-133408 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Chymotrypsin A chain A Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.25 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 1-13; Coverage: 5%)
Chymotrypsin A chain B Chain: B
Molecule details ›
Chain: B
Length: 131 amino acids
Theoretical weight: 13.93 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00766 (Residues: 16-146; Coverage: 54%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Chymotrypsin A chain C Chain: C
Molecule details ›
Chain: C
Length: 97 amino acids
Theoretical weight: 10.07 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00766 (Residues: 149-245; Coverage: 40%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Ovomucoid Chain: I
Molecule details ›
Chain: I
Length: 51 amino acids
Theoretical weight: 5.6 KDa
Source organism: Meleagris gallopavo
Expression system: Escherichia coli
UniProt:
  • Canonical: P68390 (Residues: 135-185; Coverage: 28%)
Sequence domains: Kazal-type serine protease inhibitor domain
Structure domains: Wheat Germ Agglutinin (Isolectin 2); domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P61
Unit cell:
a: 103.47Å b: 103.47Å c: 47.12Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.193 0.246
Expression system: Escherichia coli