1acb

X-ray diffraction
2Å resolution

CRYSTAL AND MOLECULAR STRUCTURE OF THE BOVINE ALPHA-CHYMOTRYPSIN-EGLIN C COMPLEX AT 2.0 ANGSTROMS RESOLUTION

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chymotrypsinogen A Chain: E
Molecule details ›
Chain: E
Length: 245 amino acids
Theoretical weight: 25.69 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00766 (Residues: 1-245; Coverage: 100%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Eglin C Chain: I
Molecule details ›
Chain: I
Length: 70 amino acids
Theoretical weight: 8.1 KDa
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
  • Canonical: P01051 (Residues: 1-70; Coverage: 100%)
Sequence domains: Potato inhibitor I family
Structure domains: Trypsin Inhibitor V, subunit A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 55.3Å b: 59.4Å c: 42.5Å
α: 90° β: 99.1° γ: 90°
R-values:
R R work R free
0.167 not available not available
Expression system: Not provided