› 5n7q

X-ray diffraction
1.45Å resolution

CRYSTAL STRUCTURE OF MATURE CATHEPSIN D FROM THE TICK IXODES RICINUS (IRCD1) IN COMPLEX WITH THE INHIBITOR PEPSTATIN A

Released:
DOI: 10.2210/pdb5n7q/pdb
PDB 5n7q coloured by chain and viewed from the front.
PDB 5n7q coloured by chain and viewed from the side.
PDB 5n7q coloured by chain and viewed from the top.
Source organisms:
Primary publication:
Novel Structural Mechanism of Allosteric Regulation of Aspartic Peptidases via an Evolutionarily Conserved Exosite.
Hánová I, Brynda J, Houštecká R, Alam N, Sojka D, Kopáček P, Marešová L, Vondrášek J, Horn M, Schueler-Furman O, Mareš M
Cell Chem Biol (2018)
PMID: 29396291

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase A1 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 339 amino acids
Theoretical weight: 36.79 KDa
Source organism: Ixodes ricinus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: V5HCK7 (Residues: 44-382; Coverage: 94%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
PEPSTATIN A Chains: I, J
Molecule details ›
Chains: I, J
Length: 6 amino acids
Theoretical weight: 686 Da
Source organism: Actinomycetes
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand PEG 1 x PEG
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21
Unit cell:
a: 61.14Å b: 82.82Å c: 61.39Å
α: 90° β: 91.13° γ: 90°
R-values:
R R work R free
0.146 0.145 0.166
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

1 review citation

Precursors of Viral Proteases as Distinct Drug Targets.
Majerová et al. (2021)
4 other articles

1 mention without citation

Partial Characterization of Two Cathepsin D Family Aspartic Peptidases of Clonorchis sinensis.
Kang et al. (2019)