› 2asi

X-ray diffraction
2.15Å resolution

ASPARTIC PROTEINASE

Released:
DOI: 10.2210/pdb2asi/pdb
PDB entry 2asi coloured by chain, front view.
PDB entry 2asi coloured by chain, side view.
PDB entry 2asi coloured by chain, top view.
Source organism: Rhizomucor miehei
Primary publication:
Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15 A resolution.
Yang J, Teplyakov A, Quail JW
J Mol Biol 268 449-59 (1997)
PMID: 9159482

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-133578 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Mucorpepsin Chain: A
Molecule details ›
Chain: A
Length: 361 amino acids
Theoretical weight: 38.74 KDa
Source organism: Rhizomucor miehei
UniProt:
  • Canonical: P00799 (Residues: 70-430; Coverage: 89%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
1 bound ligand:
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 41.857Å b: 51.209Å c: 174.244Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.281

Quick links

Citations

1 review citation

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

1 mention without citation

Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
Andreeva et al. (2001)