› 1fq5

X-ray diffraction
2.4Å resolution

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

Released:
DOI: 10.2210/pdb1fq5/pdb
PDB entry 1fq5 coloured by chain, front view.
PDB entry 1fq5 coloured by chain, side view.
PDB entry 1fq5 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
X-ray structures of five renin inhibitors bound to saccharopepsin: exploration of active-site specificity.
Cronin NB, Badasso MO, J Tickle I, Dreyer T, Hoover DJ, Rosati RL, Humblet CC, Lunney EA, Cooper JB
J Mol Biol 303 745-60 (2000)
PMID: 11061973

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.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139464 (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
Carbohydrate polymer
2 bound ligands:
Ligand NAG 1 x NAG
Ligand 0GM 1 x 0GM
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

Quick links

Citations

1 review citation

The structure and function of Saccharomyces cerevisiae proteinase A.
Parr et al. (2007)
4 other articles