PDBe 4h4f

X-ray diffraction
1.9Å resolution

Crystal structure of human chymotrypsin C (CTRC) bound to inhibitor eglin c from Hirudo medicinalis

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Chymotrypsin-C Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 28.05 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q99895 (Residues: 30-268; Coverage: 95%)
Gene names: CLCR, CTRC
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Eglin C Chain: B
Molecule details ›
Chain: B
Length: 70 amino acids
Theoretical weight: 8.07 KDa
Source organism: Hirudo medicinalis
Expression system: Escherichia coli
UniProt:
  • Canonical: P01051 (Residues: 8-70; Coverage: 90%)
Sequence domains: Potato inhibitor I family
Structure domains: Trypsin Inhibitor V, subunit A
Chymotrypsin-C Chain: Q
Molecule details ›
Chain: Q
Length: 10 amino acids
Theoretical weight: 1.03 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q99895 (Residues: 17-26; Coverage: 4%)
Gene names: CLCR, CTRC

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 56.272Å b: 76.253Å c: 81.823Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.157 0.21
Expression systems:
  • Not provided
  • Escherichia coli