› 4h4f

X-ray diffraction
1.9Å resolution

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

Released:
DOI: 10.2210/pdb4h4f/pdb
PDB entry 4h4f coloured by chain, front view.
PDB entry 4h4f coloured by chain, side view.
PDB entry 4h4f coloured by chain, top view.
Source organisms:
Primary publication:
Long-range electrostatic complementarity governs substrate recognition by human chymotrypsin C, a key regulator of digestive enzyme activation.
Batra J, Szabó A, Caulfield TR, Soares AS, Sahin-Tóth M, Radisky ES
J Biol Chem 288 9848-9859 (2013)
PMID: 23430245

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Leu-|-, Tyr-|-, Phe-|-, Met-|-, Trp-|-, Gln-|-, Asn-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133912 (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:
Ligand PO4 3 x PO4
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

Quick links

Citations

1 review citation

Purification and Biological Function of Caldecrin.
Tomomura et al. (2021)
15 other articles

15 mentions without citation

Caldecrin: A pancreas-derived hypocalcemic factor, regulates osteoclast formation and function.
Tomomura et al. (2015)
14 more