› 1ize

X-ray diffraction
1.9Å resolution

Crystal structure of Aspergillus oryzae Aspartic proteinase complexed with pepstatin

Released:
DOI: 10.2210/pdb1ize/pdb
PDB entry 1ize coloured by chain, front view.
PDB entry 1ize coloured by chain, side view.
PDB entry 1ize coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structures of Aspergillus oryzae aspartic proteinase and its complex with an inhibitor pepstatin at 1.9A resolution.
Kamitori S, Ohtaki A, Ino H, Takeuchi M
J Mol Biol 326 1503-11 (2003)
PMID: 12595261

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.
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-143554 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspergillopepsin-1 Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 33.8 KDa
Source organism: Aspergillus oryzae
UniProt:
  • Canonical: P0CU33 (Residues: 68-390; Coverage: 87%)
Gene name: pepA
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Pepstatin Chain: B
Molecule details ›
Chain: B
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 MAN 1 x MAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 106.767Å b: 38.627Å c: 78.732Å
α: 90° β: 120.31° γ: 90°
R-values:
R R work R free
0.185 0.185 0.221
Expression system: Not provided

Quick links

Citations

9 citation in other articles

Apo and inhibitor complex structures of BACE (beta-secretase).
Patel et al. (2004)
8 more