› 1wkr

X-ray diffraction
1.3Å resolution

Crystal structure of aspartic proteinase from Irpex lacteus

Released:
DOI: 10.2210/pdb1wkr/pdb
PDB entry 1wkr coloured by chain, front view.
PDB entry 1wkr coloured by chain, side view.
PDB entry 1wkr coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of aspartic proteinase from Irpex lacteus in complex with inhibitor pepstatin.
Fujimoto Z, Fujii Y, Kaneko S, Kobayashi H, Mizuno H
J Mol Biol 341 1227-35 (2004)
PMID: 15321718

Function and Biology Details

Reaction catalysed: 
Milk clotting activity, broad specificity, but fails to cleave 15-Leu-|-Tyr-16 or 16-Tyr-|-Leu-17 of insulin B chain.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148101 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Polyporopepsin Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 35.05 KDa
Source organism: Irpex lacteus
UniProt:
  • Canonical: P17576 (Residues: 1-340; Coverage: 100%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
pepstatin Chain: I
Molecule details ›
Chain: I
Length: 6 amino acids
Theoretical weight: 686 Da
Source organism: Streptomyces argenteolus subsp. toyonakensis
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 7 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 37.27Å b: 78.898Å c: 54.072Å
α: 90° β: 96.71° γ: 90°
R-values:
R R work R free
0.147 0.147 0.171
Expression system: Not provided

Quick links

Citations

1 review citation

Proteases of Wood Rot Fungi with Emphasis on the Genus Pleurotus.
Inácio et al. (2015)
8 other articles

2 mentions without citation

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