1fq5

X-ray diffraction
2.4Å resolution

X-ray structure of a cyclic statine inhibitor PD-129,541 bound to yeast proteinase A

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Saccharopepsin Chain: A
Molecule details ›
Chain: A
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, MAN, BMA
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P3221
Unit cell:
a: 87.3Å b: 87.3Å c: 110.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 not available 0.28