3apr

X-ray diffraction
1.8Å resolution

BINDING OF A REDUCED PEPTIDE INHIBITOR TO THE ASPARTIC PROTEINASE FROM RHIZOPUS CHINENSIS. IMPLICATIONS FOR A MECHANISM OF ACTION

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Rhizopuspepsin Chain: E
Molecule details ›
Chain: E
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
REDUCED PEPTIDE INHIBITOR Chain: I
Molecule details ›
Chain: I
Length: 7 amino acids
Theoretical weight: 1.08 KDa
Source organism: Rhizopus microsporus var. chinensis
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 60.37Å b: 60.61Å c: 106.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 not available not available
Expression system: Not provided