1fmx

X-ray diffraction
2.61Å resolution

STRUCTURE OF NATIVE PROTEINASE A IN THE SPACE GROUP P21

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139464 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Saccharopepsin Chains: A, B
Molecule details ›
Chains: A, B
Length: 329 amino acids
Theoretical weight: 35.77 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P07267 (Residues: 77-405; Coverage: 86%)
Gene names: P2585, PEP4, PHO9, PRA1, YPL154C
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P21
Unit cell:
a: 82.964Å b: 49.074Å c: 94.685Å
α: 90° β: 96.5° γ: 90°
R-values:
R R work R free
0.205 0.205 0.279