X-ray diffraction
2.3Å resolution

Crystal structure of rhizopuspepsin at pH 8.0

Primary publication:
Effect of pH on the structure of rhizopuspepsin.
Acta Crystallogr. D Biol. Crystallogr. 59 1755-61 (2003)
PMID: 14501114

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
Rhizopuspepsin Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 34.31 KDa
Source organism: Rhizopus microsporus var. chinensis
  • Canonical: P06026 (Residues: 69-393; Coverage: 87%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 60.372Å b: 60.583Å c: 107.359Å
α: 90° β: 90° γ: 90°
R R work R free
0.158 0.158 0.201