› 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:
DOI: 10.2210/pdb1mpp/pdb
PDB entry 1mpp coloured by chain, front view.
PDB entry 1mpp coloured by chain, side view.
PDB entry 1mpp coloured by chain, top view.
Source organism: Rhizomucor pusillus
Primary publication:
X-ray analyses of aspartic proteinases. V. Structure and refinement at 2.0 A resolution of the aspartic proteinase from Mucor pusillus.
Newman M, Watson F, Roychowdhury P, Jones H, Badasso M, Cleasby A, Wood SP, Tickle IJ, Blundell TL
J Mol Biol 230 260-83 (1993)
PMID: 8450540

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.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140585 (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:
Ligand SO4 1 x SO4
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

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Citations

1 review citation

Thermophilic fungi: their physiology and enzymes.
Maheshwari et al. (2000)
20 other articles

4 mentions without citation

A comparative study of available software for high-accuracy homology modeling: from sequence alignments to structural models.
Nayeem et al. (2006)
3 more