PDBe 1mpp

X-ray diffraction
2Å resolution

X-RAY ANALYSES OF ASPARTIC PROTEINASES. V. STRUCTURE AND REFINEMENT AT 2.0 ANGSTROMS RESOLUTION OF THE ASPARTIC PROTEINASE FROM MUCOR PUSILLUS

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins, favoring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen. 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mucorpepsin Chain: A
Molecule details ›
Chain: A
Length: 361 amino acids
Theoretical weight: 38.69 KDa
Source organism: Rhizomucor pusillus
Expression system: Not provided
UniProt:
  • Canonical: P09177 (Residues: 67-427; Coverage: 89%)
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: P21212
Unit cell:
a: 70Å b: 104Å c: 46.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.162 not available
Expression system: Not provided