PDBe 2apr

X-ray diffraction
1.8Å resolution

STRUCTURE AND REFINEMENT AT 1.8 ANGSTROMS RESOLUTION OF THE ASPARTIC PROTEINASE FROM RHIZOPUS CHINENSIS

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of insulin. 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rhizopuspepsin Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 34.07 KDa
Source organism: Rhizopus microsporus var. chinensis
Expression system: Not provided
UniProt:
  • Canonical: P06026 (Residues: 69-393; Coverage: 87%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 60.31Å b: 60.6Å c: 106.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.143 not available not available
Expression system: Not provided