1ibq

X-ray diffraction
2.14Å resolution

ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS

Released:
Source organism: Aspergillus phoenicis
Primary publication:
Structure of aspergillopepsin I from Aspergillus phoenicis: variations of the S1'-S2 subsite in aspartic proteinases.
Acta Crystallogr D Biol Crystallogr 57 948-56 (2001)
PMID: 11418762

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.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171374 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspergillopepsin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 325 amino acids
Theoretical weight: 34.22 KDa
Source organism: Aspergillus phoenicis
UniProt:
  • Canonical: Q12567 (Residues: 70-394; Coverage: 87%)
Gene name: pepA
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200H
Spacegroup: P21
Unit cell:
a: 82.19Å b: 36.62Å c: 104.94Å
α: 90° β: 113.49° γ: 90°
R-values:
R R work R free
0.21 0.221 0.269